A LIST OF TBSGC SOLVED STRUCTURES

A tabular summary of all the structures solved by the group originally sourced from the Protein Data Bank.
ORF ID Gene name Function Title Structure PDB ID Author
Rv0635,Rv0636,Rv0637 hadA,hadB,hadC Involved in fatty acid synthesis type II (fas-II) 1,3-Diarylpyrazolyl-acylsulfonamides Target HadAB/BC Complex in Mycobacterium tuberculosis . 7SVT Krieger, I.V., Sacchettini, J.C.,
Ribosome Ribosome Involved in translation mechanism, 50S ribosomal protein L32 RpmF Discovery of natural-product-derived sequanamycins as potent oral anti-tuberculosis agents. 7SFR, 5V7Q Xing, Z., Cui, Z., Zhang, J.,Yang, K., Chang, J.-Y.
Rv0014c pknB Involved in signal transduction (via phosphorylation). Thought to regulate cell division/differentiation. Can phosphorylate the peptide substrate myelin basic protein (MBP) [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr kinase, PknB 3ORP, 3ORT, 5E10, 3ORL, 5E12, 5E0Z, 5E0Y, 3ORO, 3ORM, 3ORK, 3F61, 3F69, 3ORI, 1O6Y Lombana, T.N.,Echols, N.,Good, M.C.,Thomsen, N.D.,Ng, H.-L.,Greenstein, A.E.,Falick, A.M.,King, D.S.,Alber, T.
Rv0066c icd2 Involved in the KREBS cycle [catalytic activity: isocitrate + NADP+ = 2-oxoglutarate + CO(2) + NADPH]. Structural and kinetic characterization of isocitrate dehydrogenase-2 from Mycobacterium tuberculosis 5KVU Sacchettini, J.C.,Cheng, Y.S.
Rv0099 fadD10 Function unknown but involvement in lipid degradation. Structures of Mycobacterium tuberculosis FadD10 protein reveal a new type of adenylate-forming enzyme. 4ISB, 4IR7 Liu, Z.,Ioerger, T.R.,Wang, F.,Sacchettini, J.C.
Rv0223c Rv0223c Thought to oxidize a wide variety of aliphatic and aromatic aldehydes. X-ray crystal structure of aldehyde dehydrogenase from Mycobacterium tuberculosis complexed with NAD+. 3B4W Moon, J.H.,Lyon, A.E.,Yu, M.,Hung, L.-W.,Terwilliger, T.,Kim, C.-Y.
Rv0265c Rv0265c Thought to be involved in iron transport across the membrane (import). Structure of a putative periplasmic iron siderophore binding protein (Rv0265c) from Mycobacterium tuberculosis H37Rv 4PM4 Arbing, M.A.,Chan, S.,Tran, N.,Kuo, E.,Lu, J.,Harris, L.R.,Zhou, T.T.,Eisenberg, D.
Rv0287 esxG Function unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3Q4H Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Rv0288 esxH Function unknown. May be involved in virulence. Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3Q4H Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Rv0390 Rv0390 Function unknown Crystal Structure of Rv0390 from Mycobacterium tuberculosis 2FSX Bursey, E.H.,Radhakannan, T.,Yu, M.,Segelke, B.W.,Lekin, T.,Toppani, D.,Chang, Y.-B.,Kaviratne, T.,Woodruff, T.,Terwilliger, T.C.,Hung, L.-W.
Rv0407 fgd1 Catalyzes oxidation of glucose-6-phosphate to 6-phosphogluconolactone using coenzyme F420 (an *-hydroxy-5-deazaflavin derivative) as the electron acceptor. Crystal structures of F420-dependent glucose-6-phosphate dehydrogenase FGD1 involved in the activation of the anti-tuberculosis drug candidate PA-824 reveal the basis of coenzyme and substrate binding 3B4Y Bashiri, G.,Squire, C.J.,Moreland, N.J.,Baker, E.N.
Rv0467 icl1 Involved in glyoxylate bypass (at the first step) an alternative to the tricarboxylic acid cycle (in bacteria plants and fungi) [catalytic activity: isocitrate = succinate + glyoxylate]. Involved in the persistence in the host. Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. 1F61, 1F8M, 1F8I, 7RB1, 5DQL, 6VB9, 6WSI Sharma, V.,Sharma, S.,Hoener zu Bentrup, K.,McKinney, J.D.,Russell, D.G.,Jacobs Jr., W.R.,Krieger, I.V., Mellott, D., Meek, T., Sacchettini, J.C.
Rv0470c pcaA Involved in the mycolic acid modification or synthesis; essential for the cyclopropanation function. Required for cording and mycolic acid cyclopropane ring synthesis in the cell wall. Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis. 1L1E Huang, C.-C.,Smith, C.V.,Glickman, M.S.,Jacobs Jr., W.R.,Sacchettini, J.C.
Rv0489 gpm1 Involved in glycolysis [catalytic activity: 1 3-diphosphoglycerate + 3-phosphoglycerate = 2 3-diphosphoglycerate + 3-phosphoglycerate]. The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. 1RII Muller, P.,Sawaya, M.R.,Pashkov, I.,Chan, S.,Nguyen, C.,Wu, Y.,Perry, L.J.,Eisenberg, D.
Rv0503c cmaA2 Essential for the cyclopropanation function. Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. Mycolic acids which represent the major constituent of mycobacterial cell wall complex act as substrates [catalytic activity: S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid]. Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis 1KPI, 3HEM Huang, C.C.,Smith, C.V.,Glickman, M.S.,Jacobs Jr., W.R., Liu, Z.,Sacchettini, J.C. J.C.
Rv0533c fabH Involved in fatty acid biosynthesis. Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. KAS III catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities [catalytic activity: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]]. Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. 1M1M, 2AJ9, 2AHB Brown, A.K.,Sridharan, S.,Kremer, L.,Lindenberg, S.,Dover, L.G.,Sacchettini, J.C.,Besra, G.S.
Rv0548c menB Involved in menaquinone biosynthesis. Convert O-succinylbenzoyl-CoA (OSB-CoA) to 1 4-dihydroxy-2-naphthoic acid (DHNA) [catalytic activity: O-succinylbenzoyl-CoA = 1 4-dihydroxy-2-naphthoate + CoA]. Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms. 1RJM, 1Q52, 1Q51 Johnston, J.M.,Arcus, V.L.,Baker, E.N.
Rv0577 TB27.3 Function unknown. Involved in ability to absorb neutral red stain. Structural and Biophysical Characterization of the Mycobacterium tuberculosis Protein Rv0577, a Protein Associated with Neutral Red Staining of Virulent Tuberculosis Strains and Homologue of the Streptomyces coelicolor Protein KbpA. 3OXH Buchko, G.W.,Echols, N.,Flynn, E.M.,Ng, H.L.,Stephenson, S.,Kim, H.B.,Myler, P.J.,Terwilliger, T.C.,Alber, T.,Kim, C.Y.
Rv0626 vapB5 Possible ribonuclease Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems: VapBC-5 FROM MYCOBACTERIUM TUBERCULOSIS. 3DBO Miallau, L.,Faller, M.,Chiang, J.,Arbing, M.,Guo, F.,Cascio, D.,Eisenberg, D.
Rv0627 vapC5 Unknown Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems: VapBC-5 FROM MYCOBACTERIUM TUBERCULOSIS. 3DBO Miallau, L.,Faller, M.,Chiang, J.,Arbing, M.,Guo, F.,Cascio, D.,Eisenberg, D.
Rv0632c echA3 Could possibly oxidize fatty acids using specific components [catalytic activity: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O]. Crystal structure and mechanism of the prokaryotic enoyl CoA isomerase 4FND, 4FNB, 4FN8, 4FN7 Bruning, J.B.,Gao, N.,Hernandez, E.D.,Li, H.,Dang, N.,Hung, L.W.,Moran, S.,Sacchettini, J.C.
Rv0667 rpoB Catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates [catalytic activity: N nucleoside triphosphate = N diphosphate + {RNA}(N)]. Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD. 4KBM, 4KBJ Gulten, G.,Sacchettini, J.C.
Rv0931c pknD Involved in signal transduction (via phosphorylation). Thought to regulate phosphate transport. Can phosphorylate the peptide substrate myelin basic protein (MBP) at serine and threonine residues. Can be autophosphorylated on threonine residues [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. Sensor Domain of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknD, forms a Highly Symmetric beta Propeller. 1RWL, 1RWI Good, M.C.,Greenstein, A.E.,Young, T.A.,Ng, H.L.,Alber, T.
Rv0983 pepD Function unknown; possibly hydrolyzes peptides and/or proteins (seems to cleave preferentially after serine residues). Possible role for HtrA homologs in mycobacterium tuberculosis 1Y8T, 2Z9I Palaninathan, S.K.,MohamedMohaideen, N.N.,Sacchettini, J.C.
Rv1018c glmU Peptidoglycan and lipopolysaccharide biosynthesis Structure and function of GlmU from Mycobacterium tuberculosis. 2QKX Zhang, Z.,Bulloch, E.M.,Bunker, R.D.,Baker, E.N.,Squire, C.J.
Rv1070c echA8 Could possibly oxidize fatty acids using specific components [catalytic activity: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O]. Crystal Structure and Mechanism of the Prokaryotic Crotonase 4FJW, 3Q0J, 3PZK, 3Q0G Bruning, J.B.,Delgado, E.,Ghosh, S.,Sacchettini, J.C.
Rv1098c fum Involved in the tricarboxylic acid cycle. Catalyzes the reversible hydration of fumarate to L-malate [catalytic activity: (S)-malate = fumarate + H2O] Crystal Structure of apo fumarate hydratase from Mycobacterium tuberculosis 3NO9 Li, H.,Swanson, S.,Yu, M.,Hung, L.-H.,Sacchettini, J.S.
Rv1102c mazF3 Sequence-specific mRNA cleavage Crystal structure of Mtb toxin 5CCA Cascio, D.,Arbing, M.,de Serrano, V.,Eisenberg, D.,Miallau, L.,TB Structural Genomics Consortium (TBSGC)
Rv1240 mdh Involved in the conversion of malate to oxaloacetate [catalytic activity: (S)-malate + NAD+ = oxaloacetate + NADH]. Structure of Malate Dehydrogenase in complex with NADH from Mycobacterium tuberculosis 5KVV Cheng, Y.S.,Sacchettini, J.C.
Rv1346 mbtN Thought to be involved in the biogenesis of the hydroxyphenyloxazoline-containing siderophore mycobactins A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket. 4XVX Chai, A.F.,Bulloch, E.M.,Evans, G.L.,Lott, J.S.,Baker, E.N.,Johnston, J.M.
Rv1347c mbtK Involved in the biogenesis of the hydroxyphenyloxazoline-containing siderophore mycobactins The crystal structure of Rv1347c, a putative antibiotic resistance protein from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests an alternative function in siderophore biosynthesis 1YK3 Card, G.L.,Peterson, N.A.,Smith, C.A.,Rupp, B.,Schick, B.M.,Baker, E.N.
Rv1389 gmk Essential for recycling GMP and indirectly CGMP [catalytic activity: ATP + GMP = ADP + GDP] Crystal Structure of Guanylate Kinase from Mycobacterium tuberculosis 1S4Q, 1Z8F Chan, S.,Sawaya, M.R.,Perry, L.J.,Eisenberg, D.
Rv1404 Rv1404 Involved in transcriptional mechanism Crystal structure of RV1404 from Mycobacterium tuberculosis 2NYX Yu, M.,Bursey, E.H.,Radhakannan, R.,Kim, C.-Y.,Kaviratne, T.,Woodruff, T.,Segelke, B.W.,Lekin, T.,Toppani, D.,Terwilliger, T.C.,Hung, L.-W.
Rv1411c lprG Unknown Mycobacterium tuberculosis lipoprotein LprG (Rv1411c) binds triacylated glycolipid agonists of Toll-like receptor 2. 3MH8, 4ZRA, 3MHA, 3MH9 Drage, M.G.,Tsai, H.C.,Pecora, N.D.,Cheng, T.Y.,Arida, A.R.,Shukla, S.,Rojas, R.E.,Seshadri, C.,Moody, D.B.,Boom, W.H.,Sacchettini, J.C.,Harding, C.V.
Rv1596 nadC de novo biosynthesis of NAD and NADP [catalytic activity: nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2 3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate] Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target. 1QPQ, 1QPO, 1QPN, 1QPR Sharma, V.,Grubmeyer, C.,Sacchettini, J.C.
Rv1611 trpC Tryptophan biosynthesis pathway (fourth step) [catalytic activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-(indol-3-YL)glycerol 3-phosphate + CO(2) + H(2)O.] Structural Insights and Inhibition of Mycobacterium tuberculosis Indole Glycerol Phosphate Synthase (IGPS): an Essential Enzyme for Tryptophan Biosynthesis 3T78, 3T55, 3T44, 3T40, 4FB7, 3QJA Reddy, M.C.M., Bruning, J.B., Thurman, C.,Michalska, K., Chhor, G., Jedrzejczak, R., Terwilliger, T.C., Rubin, E.J., Guinn, K., Baker, D., Ioerger, T.R., Sacchettini, J.C., Joachimiak, A.
Rv1747 Rv1747 Thought to be involved in active transport of undetermined substrate (possibly lipooligosaccharide) across the membrane. Responsible for energy coupling to the transport system and for the translocation of the substrate across the membrane. Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. 6CCD Heinkel, F.,Shen, L.,Richard-Greenblatt, M.,Okon, M.,Bui, J.M.,Gee, C.L.,Gay, L.M.,Alber, T.,Av-Gay, Y.,Gsponer, J.,McIntosh, L.P.
Rv1821 secA2 Involved in protein export. May interact with the SECY/SECE subunits. SECA has a central role in coupling the hydrolysis of ATP to the transfer of PRE-secretory periplasmic and outer membrane proteins across the membrane. Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2. 4UAQ Swanson, S.,Ioerger, T.R.,Rigel, N.W.,Miller, B.K.,Braunstein, M.,Sacchettini, J.C.
Rv1837c glcB Involved in glyoxylate bypass (second step) an alternative to the tricarboxylic acid cycle [catalytic activity: L-malate + CoA = acetyl-CoA + H(2)O + glyoxylate] Anion-pi Interactions in Computer-Aided Drug Design: Modeling the Inhibition of Malate Synthase by Phenyl-Diketo Acids. 6AXB, 6ASU, 6AU9, 6AS6, 6APZ, 6BA7, 6BU1, 6C2X, 6C8P, 6C6O, 6C7B, 6DNP, 6DLJ, 6DL9, 6DKO, 5E9X, 5ECV, 5H8M, 5H8P, 5H8U, 5DX7, 5DRC, 5DRI, 5C7V, 5C9U, 5C9W, 5C9X, 5CAH, 5CAK, 5CBB, 5CBI, 5CBJ, 5CC3, 5CC5, 5CC6, 5CC7, 5CCZ, 5CEW, 5CJM, 5CJN, 5C9R, 3S9I, 3S9Z, 3SAD, 3SAZ, 3SB0, 1N8W, 1N8I Ellenbarger, J.F.,Krieger, I.V.,Huang, H.L.,Gomez-Coca, S.,Ioerger, T.R.,Sacchettini, J.C.,Wheeler, S.E.,Dunbar, K.R.
Rv1848 ureA Involved in the conversion of urea to NH3 [catalytic activity: urea + H2O = CO2 + 2 NH3] Crystal Structure of Rv1848, a Urease Gamma Subunit UreA (Urea amidohydrolase), from Mycobacterium Tuberculosis 2FVH Bursey, E.H.,Yu, M.,Segelke, B.W.,Lekin, T.,Rupp, B.,Kim, C.Y.,Rho, B.S.,Terwilliger, T.C.,Hung, L.-W.
Rv1876 bfrA Involved in iron storage (may perform analogous functions in iron detoxification and storage as that of animal ferritins); ferritin is an intracellular molecule that stores iron in a soluble nontoxic readily available form. The functional molecule which is composed of 24 chains is roughly spherical and contains a central cavity in which the polymeric ferric iron core is deposited. Mycobacterium tuberculosis bacterioferritin, BfrA 3UOI, 3UOF, 3QB9 McMath, L.M.,Goulding, C.W.
Rv1926c mpt63 Unknown Crystal structure of a major secreted protein of Mycobacterium tuberculosis-MPT63 at 1.5-A resolution 1LMI Goulding, C.W.,Parseghian, A.,Sawaya, M.R.,Cascio, D.,Apostol, M.,Gennaro, M.L.,Eisenberg, D.
Rv1932 tpx Has antioxidant activity. Could remove peroxides or H(2)O(2) Functional and Structural Characterization of a Thiol Peroxidase from Mycobacterium tuberculosis. 1XVQ Rho, B.S.,Hung, L.W.,Holton, J.M.,Vigil, D.,Kim, S.I.,Park, M.S.,Terwilliger, T.C.,Pedelacq, J.D.
Rv2068c blaC Hydrolyses beta-lactams to generate corresponding beta-amino acid [catalytic activity: a beta-lactam + H(2)O = a substituted beta-amino acid]. Faropenem is Effective Against Mycobacterium tuberculosis in vitro and in vivo 4EBP, 4EBN, 4EBL, 3VFH, 3VFF, 2GDN Mire, J.A.,Pai, P.,Siddiqi, N.,Russell, D.H.,Rubin, E.J.,Sacchettini, J.C.
Rv2121c hisG Involved in histidine biosynthesis. Crystal Structure of ATP Phosphoribosyltransferase from Mycobacterium Tuberculosis 1NH7, 1NH8 Cho, Y.,Sharma, V.,Sacchettini, J.C.
Rv2122c hisE Involved in histidine biosynthesis. The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis. 3C90, 1Y6X Javid-Majd, F.,Yang, D.,Ioerger, T.R.,Sacchettini, J.C.
Rv2192c trpD Tryptophan biosynthesis Binding and mimicking of the phosphate-rich substrate, PRPP 5C2L, 5BYT, 5BO3, 5BO2, 5BNE, 4ZTV, 4ZOK, 4ZOJ, 4ZOF, 3QSA, 3QS8, 3QQS, 1ZVW, 5C7S, 5C1R, 4M0R, 4IJ1, 4GKM, 4GIU, 3R6C, 3QR9, 2BPQ Evans, G.L.,Baker, E.N.,Lott, J.S.
Rv2202c adoK Adenosine phosphorylation Structure-Guided Drug Design of 6-Substituted Adenosine Analogues as Potent Inhibitors of Mycobacterium tuberculosis Adenosine Kinase. 6C9S, 6C9Q, 2PKN, 2PKK, 6C9V, 6C9R, 6C9P, 6C9N, 6C67, 4UBE Crespo, R.A.,Dang, Q.,Zhou, N.E.,Guthrie, L.M.,Snavely, T.C.,Dong, W.,Loesch, K.A.,Suzuki, T.,You, L.,Wang, W.,O'Malley, T.,Parish, T.,Olsen, D.B.,Sacchettini, J.C.
Rv2225 panB Involved in pantothenate biosynthesis. The Crystal Structure of the First Enzyme in the Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase, from M. tuberculosis 1OY0 Chaudhuri, B.N.,Sawaya, M.R.,Kim, C.Y.,Waldo, G.S.,Park, M.S.,Terwilliger, T.C.,Yeates, T.O.
Rv2238c ahpE Detoxification of organic peroxides. Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys Peroxiredoxin 1XXU, 1XVW Li, S.,Peterson, N.A.,Kim, M.Y.,Kim, C.Y.,Hung, L.W.,Yu, M.,Lekin, T.,Segelke, B.W.,Lott, J.S.,Baker, E.N.
Rv2246 kasB Involved in fatty acid biosynthesis (mycolic acids synthesis); involved in meromycolate extension. Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP [catalytic activity: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + [acyl-carrier protein] + CO(2)]. X-Ray Crystal Structure of Mycobacterium tuberculosis beta-Ketoacyl Acyl Carrier Protein Synthase II (mtKasB). 2GP6 Sridharan, S.,Wang, L.,Brown, A.K.,Dover, L.G.,Kremer, L.,Besra, G.S.,Sacchettini, J.C.
Rv2247 accD6 Involved in fatty acid biosynthesis (mycolic acids synthesis) [catalytic activity: ATP + propionyl-CoA + CO(2) + H(2)O = ADP + orthophosphate + methylmalonyl-CoA]. Novel herbicidal derivatives that inhibit carboxyltransferase subunit of the acetyl-CoA carboxylase in Mycobacterium tuberculosis 6TZV, 6PRW, 6PK2, 4FB8, 4G2R, 6P7U Reddy, M.C.M.,Zhou, N.,Sacchettini, J.C.
Rv2302 Rv2302 Function unknown Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis. 2A7Y Buchko, G.W.,Kim, C.Y.,Terwilliger, T.C.,Kennedy, M.A.
Rv2346c esxO Function unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3OGI, 4GZR Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Rv2347c esxP Function unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3OGI, 4GZR Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Rv2386c mbtI Involved in the biogenesis of the hydroxyphenyloxazoline-containing siderophore mycobactins. Possibly plays a role in the conversion of chorismate to salicilate (the starter unit for mycobactin siderophore construction). Implications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosis 3ST6, 3RV9, 3RV8, 3RV7, 3RV6, 3VEH, 2G5F Chi, G.,Manos-Turvey, A.,O'Connor, P.D.,Johnston, J.M.,Evans, G.L.,Baker, E.N.,Payne, R.J.,Lott, J.S.,Bulloch, E.M.
Rv2420c Rv2420c Function unknown Structure of Ribosomal Silencing Factor Bound to Mycobacterium tuberculosis Ribosome. 4WCW Li, X.,Sun, Q.,Jiang, C.,Yang, K.,Hung, L.W.,Zhang, J.,Sacchettini, J.C.
Rv2430c PPE41 Function unknown Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. 2G38 Strong, M.,Sawaya, M.R.,Wang, S.,Phillips, M.,Cascio, D.,Eisenberg, D.
Rv2431c PE25 Function unknown Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. 2G38 Strong, M.,Sawaya, M.R.,Wang, S.,Phillips, M.,Cascio, D.,Eisenberg, D.
Rv2498c citE Interconversion of acetate and oxaloacetate from citrate [catalytic activity: citrate = acetate + oxaloacetate]. The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function. 1Z6K, 1U5V, 1U5H Goulding, C.W.,Bowers, P.M.,Segelke, B.,Lekin, T.,Kim, C.Y.,Terwilliger, T.C.,Eisenberg, D.
Rv2537c aroD Involved at the third step in the biosynthesis of chorismate within the biosynthesis of aromatic amino acids (the shikimate pathway). Catalyze a trans-dehydration via an enolate intermediate [catalytic activity: 3-dehydroquinate = 3-dehydroshikimate + H(2)O]. Structural investigation of inhibitor designs targeting 3-dehydroquinate dehydratase from the shikimate pathway of Mycobacterium tuberculosis. 3N8K, 3N59, 3N76, 3N7A, 3N86, 3N87, 3N8N Dias, M.V.,Snee, W.C.,Bromfield, K.M.,Payne, R.J.,Palaninathan, S.K.,Ciulli, A.,Howard, N.I.,Abell, C.,Sacchettini, J.C.,Blundell, T.L.
Rv2552c aroE Possibly involved at the fourth step in the biosynthesis of chorismate within the biosynthesis of aromatic amino acids (the shikimate pathway) [catalytic activity: shikimate + NADP(+) = 5-dehydroshikimate + NADPH]. Structure of Mycobacterium tuberculosis Shikimate Dehydrogenase 4P4N, 4P4L, 4P4G Lalgondar, M.,Sacchettini, J.C.
Rv2671 ribD Involved in riboflavin biosynthesis (at the second and third steps). Converts 2 5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2 4(1H 3H)-pyrimidinedione 5'-phosphate [catalytic activity 1: 2 5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5-phosphoribosylamino)uracil + NH(3)] [catalytic activity 2: 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH]. Structural Insights into Mycobacterium tuberculosis Rv2671 Protein as a Dihydrofolate Reductase Functional Analogue Contributing to para-Aminosalicylic Acid Resistance. 4XT6, 4XT5, 4XRB, 4XT8, 4XT4, 4XT7 Cheng, Y.S.,Sacchettini, J.C.
Rv2717c Rv2717c Function unknown Crystal structure of Rv2717c from Mycobacterium tuberculosis 2FR2 Hung, L.W.,Yu, M.,Bursey, E.H.,Radhakannan, T.,Segelke, B.W.,Lekin, T.,Chang, Y.B.,Terwilliger, T.C.,Kaviratne, A.,Woodruff, T.
Rv2763c dfrA Essential step for de novo glycine and purine synthesis DNA precursor synthesis and for the conversion of dUMP to dTMP [catalytic activity: 5 6 7 8-tetrahydrofolate + NADP(+) = 7 8-dihydrofolate + NADPH]. Selective inhibitors for dihydrofolate reductase from mycobacterium tuberculosis 4M2X Jung, H.,Sacchettini, J.C.
Rv2764c thyA Involved in deoxyribonucleotide biosynthesis. Provides the sole de novo source of dTMP for DANA biosynthesis [catalytic activity: 5 10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP]. Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: Insights into the selectivity and mode of inhibition 4FOX, 4FOG, 4FOA, 4FQS, 3QJ7 Reddy, M.C.M.,Bruning, J.B.,Sacchettini, J.C.,Harshbarger, W.
Rv2794c pptT Biosynthesis of fatty acids and lipids. Transfers the 4'-phosphopantetheine moiety from coenzyme A to a SER of acyl-carrier protein. Catalyzes the formation of holo-ACP which mediates the transfer of acyl fatty-acid intermediates during the biosynthesis of fatty acids and lipids [catalytic activity: CoA + APO-[acyl-carrier protein] = adenosine 3' 5'-bisphosphate + holo-[acyl-carrier protein] ]. In Vitro and In Vivo Inhibition of the Mycobacterium tuberculosis Phosphopantetheinyl Transferase PptT by Amidinoureas. 7N8E, 7N8M, 7N8L, 6CT5, Ottavi, S.,Scarry, S.M.,Mosior, J.,Ling, Y.,Roberts, J.,Singh, A.,Zhang, D.,Goullieux, L.,Roubert, C.,Bacque, E.,Lagiakos, H.R.,Vendome, J.,Moraca, F.,Li, K.,Perkowski, A.J.,Ramesh, R.,Bowler, M.M.,Tracy, W.,Feher, V.A.,Sacchettini, J.C.,Gold, B.S.,Nathan, C.F.,Aube, J.
Rv2795c Rv2795c Function unknown Structural insights into phosphopantetheinyl hydrolase PptH from Mycobacterium tuberculosis. 6UNC Mosior, J.,Bourland, R.,Soma, S.,Nathan, C.,Sacchettini, J.
Rv2844 Rv2844 Function unknown Crystal structure of a conserved hypothetical protein, rv2844, from Mycobacterium tuberculosis 2IB0 Yu, M.,Bursey, E.H.,Radhakannan, T.,Kim, C.Y.,Kaviratne, T.,Woodruff, T.,Segelke, B.W.,Lekin, T.,Toppani, D.,Terwilliger, T.C.,Hung, L.W.
Rv2865 relF Function unknown The crystal structure of the toxin-antitoxin complex RelBE2 (Rv2865-2866) from Mycobacterium tuberculosis 3G5O Miallau, L.,Chernishof, I.,Chiang, J.,Arbing, M.,Cascio, D.,Eisenberg, D.
Rv2866 relG Function unknown The crystal structure of the toxin-antitoxin complex RelBE2 (Rv2865-2866) from Mycobacterium tuberculosis 3G5O Miallau, L.,Chernishof, I.,Chiang, J.,Arbing, M.,Cascio, D.,Eisenberg, D.
Rv2874 dipZ Could be involved in cytochrome-C biogenesis. Structure of the C-terminal domain of DipZ from Mycobacterium tuberculosis 2HYX Goldstone, D.,Baker, E.N.,Metcalf, P.
Rv2878c mpt53 Not really known. Despite a weak homology to thioredoxin this cannot serve as a substrate for thioredoxin reductase. Furthermore it has no disulfide reducing activity. Gram-positive DsbE Proteins Function Differently from Gram-negative DsbE Homologs: A STRUCTURE TO FUNCTION ANALYSIS OF DsbE FROM MYCOBACTERIUM TUBERCULOSIS. 1LU4 Goulding, C.W.,Apostol, M.I.,Gleiter, S.,Parseghian, A.,Bardwell, J.,Gennaro, M.,Eisenberg, D.
Rv2911 dacB2 Involved in peptidoglycan synthesis (at final stages). Hydrolyzes the bound D-alanyl-D-alanine [catalytic activity: D-alanyl-D-alanine + H(2)O = 2 D-alanine]. Subfamily-Specific Adaptations in the Structures of Two Penicillin-Binding Proteins from Mycobacterium tuberculosis. 4P0M, 4RYE Prigozhin, D.M.,Krieger, I.V.,Huizar, J.P.,Mavrici, D.,Waldo, G.S.,Hung, L.,Sacchettini, J.C.,Terwilliger, T.C.,Alber, T., Cuff, M., Tan, K., Hatzos-Skintges, C., Jedrzejczak, R., Joachimiak, A.
Rv2919c glnB In nitrogen-limiting conditions when the ratio of GLN to 2-ketoglutarate decreases P-II is uridylylated to P-II-UMP by GLND|Rv2918c. P-II-UMP allows the deadenylylation of glutamine synthetase (gs) thus activating the enzyme. Converserly in nitrogen excess P-II is deuridylated and promotes the adenylation of gs. P-II indirectly controls the transcription of the gs gene (GLNA: four copies in the genome). P-II prevents NR-II catalyzed conversion of NR-I to NR-I-phosphate the transcriptional activator of GLNA. When P-II is uridylylated to P-II-UMP these events are reversed. Crystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII protein. 3LF0, 3BZQ Shetty, N.D.,Reddy, M.C.,Palaninathan, S.K.,Owen, J.L.,Sacchettini, J.C.
Rv2981c ddlA Involved in cell wall formation. Along with alanine racemase it MAKES up the D-alanine branch of the peptidoglycan biosynthetic route. [catalytic activity: ATP + D-alanine + D-alanine = ADP + phosphate + D-alanyl-D-alanine]. Structure of the Mycobacterium tuberculosis D-Alanine:D-Alanine Ligase, a Target of the Antituberculosis Drug D-Cycloserine. 3LWB Bruning, J.B.,Murillo, A.C.,Chacon, O.,Barletta, R.G.,Sacchettini, J.C.
Rv2996c serA1 Involved at the first committed step in the 'phosphorylated' pathway of L-serine biosynthesis [catalytic activity: 3-phosphoglycerate + NAD(+) = 3-phosphohydroxypyruvate + NADH]. Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase: EXTREME ASYMMETRY IN A TETRAMER OF IDENTICAL SUBUNITS 1YGY, 3DC2, 3DDN Dey, S.,Grant, G.A.,Sacchettini, J.C.
Rv3019c esxR Unknown Crystal structure of Rv3019c-Rv3020c from Mycobacterium tuberculosis 3H6P Chan, S.,Arbing, M.,Phan, T.,Kaufmann, M.,Cascio, D.,Eisenberg, D.
Rv3020c esxS Function unknown Crystal structure of Rv3019c-Rv3020c from Mycobacterium tuberculosis 3H6P Chan, S.,Arbing, M.,Phan, T.,Kaufmann, M.,Cascio, D.,Eisenberg, D.
Rv3248c sahH Thioester hydrolase which acting on ether bounds. Could be involved in methionine and selenoamino acid metabolisms. Also involved in activated methyl. Cycle adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine [catalytic activity: S-adenosyl-L-homocysteine + H(2)O = adenosine + L-homocysteine]. Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with substrate and inhibitors. 3DHY, 2ZIZ, 2ZJ0, 2ZJ1, 3CE6 Reddy, M.C.M., Gokulan, K., Shetty, N.D., Owen, J.L., Ioerger, T.R., Sacchettini, J.C.
Rv3275c purE Involved in purine biosynthesis (sixth step). This subunit can alone transform air to CAIR but in association with PURK which possesses an ATPase activity an enzyme complex is produced which is capable of converting air to CAIR efficiently under physiological condition [catalytic activity: 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate = 1-(5-phosphoribosyl)-5-aminoimidazole + CO(2)]. Crystal Structure of Rv3275c-E60A from Mycobacterium tuberculosis at 1.7A Resolution 3LP6 Kim, H.,Yu, M.,Hung, L.-W.,Terwilliger, T.C.,Kim, C.-Y.
Rv3291c lrpA Involved in transcriptional mechanism. Crystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation response. 2QZ8 Reddy, M.C.,Gokulan, K.,Jacobs, W.R.,Ioerger, T.R.,Sacchettini, J.C.
Rv3330 dacB1 Involved in peptidoglycan synthesis (at final stages). Hydrolyzes the bound D-alanyl-D-alanine [catalytic activity: D-alanyl-D-alanine + H(2)O = 2 D-alanine]. Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. 4PPR Prigozhin, D.M.,Krieger, I.V.,Huizar, J.P.,Mavrici, D.,Waldo, G.S.,Hung, L.W.,Sacchettini, J.C.,Terwilliger, T.C.,Alber, T.
Rv3356c folD Necessary for the biosynthesis of purines thymydylate methionine histidine pantothenate and formyl tRNA-met [catalytic activity: 5 10-methylenetetrahydrofolate + NADP(+) = 5 10-methenyltetrahydrofolate + NADPH] [catalytic activity: 5 10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate]. Three Dimensional Structure of Bifunctional Methylenetetrahydrofolate Dehydrogenase-Cyclohydrolase from Mycobacterium tuberculosis 2C2Y, 2C2X Javid-Majd, F.,Sacchettini, J.C.
Rv3357 relJ Function unknown Crystal structure of Mycobacterium tuberculosis RelJK (Rv3357-Rv3358-RelBE3) 3OEI Miallau, L.,Cascio, D.,Eisenberg, D.
Rv3358 relK Function unknown Crystal structure of Mycobacterium tuberculosis RelJK (Rv3357-Rv3358-RelBE3) 3OEI Miallau, L.,Cascio, D.,Eisenberg, D.
Rv3392c cmaA1 Has cyclopropane function. Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. Mycolic acids which represent the major constituent of mycobacterial cell wall complex act as substrates [catalytic activity: S-adenosyl-L-methionine + phospholipidolefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid]. Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis 1KPG, 1KPH, 1KP9 Huang, C.-C.,Smith, C.V.,Glickman, M.S.,Jacobs Jr., W.R.,Sacchettini, J.C.
Rv3574 kstR Involved in transcriptional mechanism. Predicted to control regulon involved in lipid metabolism Crystal structure of KstR in complex with cognate DNA operator 5UA2, 5UA1, 5CXI, 5CXG, 3MNL, 5CW8 Ho, N.A.T.,Dawes, S.S.,Baker, E.N.,Lott, J.S.
Rv3582c ispD Involved in the deoxyxylulose-5-phosphate pathway (DXP) of isoprenoid biosynthesis (at the third step). Catalyzes the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol (CDP-me) from CTP and 2C-methyl-D-erythritol 4-phosphate (MEP). Crystal Structure of Mycobacterium tuberculosis 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD): a candidate antitubercular drug target 3Q80, 3Q7U, 3OKR Reddy, M.C.M.,Bruning, J.B.,Thurman, C.,Ioerger, T.R.,Sacchettini, J.C.
Rv3583c Rv3583c Involved in transcriptional mechanism. Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD. 4KBM Gulten, G.,Sacchettini, J.C.
Rv3601c panD Involved in pantothenate biosynthesis [catalytic activity: L-aspartate = beta-alanine + CO(2)]. The molecular basis of pyrazinamide activity on Mycobacterium tuberculosis PanD. 6P1Y, 6P02, 6OZ8, 6OYY Sun, Q.,Li, X.,Perez, L.M.,Shi, W.,Zhang, Y.,Sacchettini, J.C.
Rv3602c panC Involved in pantothenate biosynthesis [catalytic activity: ATP + (R)-pantoate + beta-alanine = AMP + pyrophosphate + (R)-pantothenate]. Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate 1N2O, 2A88, 2A84, 2A7X, 2A86, 1N2J, 1N2I, 1N2H, 1N2G, 1N2E, 1N2B, 1MOP Wang, S.,Eisenberg, D.
Rv3676 crp Involved in transcriptional mechanism. Structural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein. 3I59, 3I54 Reddy, M.C.,Palaninathan, S.K.,Bruning, J.B.,Thurman, C.,Smith, D.,Sacchettini, J.C.
Rv3717 Rv3717 Function unknown Structural and Biochemical Analyses of Mycobacterium tuberculosis N-Acetylmuramyl-L-alanine Amidase Rv3717 Point to a Role in Peptidoglycan Fragment Recycling. 4M6I, 4M6H, 4M6G Prigozhin, D.M.,Mavrici, D.,Huizar, J.P.,Vansell, H.J.,Alber, T.
Rv3763 lpqH Shown to inhibit gamma interferon regulated HLA-DR protein and mRNA expression in human macrophages Crystal Structure of Mycobacterium tuberculosis LpqH (Rv3763) 4ZJM Arbing, M.A.,Chan, S.,Kuo, E.,Harris, L.R.,Zhou, T.T.,Eisenberg, D.
Rv3804c fbpA Involved in cell wall mycoloylation. Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor) a dominant structure necessary for maintaining cell wall integrity. Mycobacterium tuberculosis Antigen 85A and 85C Structures Confirm Binding Orientation and Conserved Substrate Specificity 1SFR Ronning, D.R.,Vissa, V.,Besra, G.S.,Belisle, J.T.,Sacchettini, J.C.
Rv3841 bfrB Involved in iron storage; ferritin is an intracellular molecule that stores iron in a soluble nontoxic readily available form. The functional molecule which is composed of 24 chains is roughly spherical and contains a central cavity in which the polymeric ferric iron core is deposited. Mycobacterium tuberculosis ferritin homolog, BfrB 3UNO, 3OJ5 McMath, L.M.,Contreras, H.,Goulding, C.W.
Rv3869 eccB1 Unknown Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. 5CYU Wagner, J.M.,Chan, S.,Evans, T.J.,Kahng, S.,Kim, J.,Arbing, M.A.,Eisenberg, D.,Korotkov, K.V.
Rv3902c Rv3902c Unknown 1.55 angstrom resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis. 4O6G Reddy, B.G.,Moates, D.B.,Kim, H.B.,Green, T.J.,Kim, C.Y.,Terwilliger, T.C.,Delucas, L.J.
Rv3910 Rv3910 Unknown A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. 3UQC Gee, C.L.,Papavinasasundaram, K.G.,Blair, S.R.,Baer, C.E.,Falick, A.M.,King, D.S.,Griffin, J.E.,Venghatakrishnan, H.,Zukauskas, A.,Wei, J.R.,Dhiman, R.K.,Crick, D.C.,Rubin, E.J.,Sassetti, C.M.,Alber, T.
MAB_1250c fumC unknown Crystal Structure of apo fumarate hydratase from Mycobacterium tuberculosis 3NO9 Li, H.,Swanson, S.,Yu, M.,Hung, L.-H.,Sacchettini, J.S.
MAB_1622 rsfS unknown Structure of Ribosomal Silencing Factor Bound to Mycobacterium tuberculosis Ribosome. 4WCW Li, X.,Sun, Q.,Jiang, C.,Yang, K.,Hung, L.W.,Zhang, J.,Sacchettini, J.C.
MAB_3112 MAB_3112 unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 4I0X Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
MAB_3113 MAB_3113 unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 4I0X Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
MAB_3286c ddl unknown Structure of the Mycobacterium tuberculosis D-Alanine:D-Alanine Ligase, a Target of the Antituberculosis Drug D-Cycloserine. 3LWB Bruning, J.B.,Murillo, A.C.,Chacon, O.,Barletta, R.G.,Sacchettini, J.C.
MAB_4049c gpmA unknown The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. 1RII Muller, P.,Sawaya, M.R.,Pashkov, I.,Chan, S.,Nguyen, C.,Wu, Y.,Perry, L.J.,Eisenberg, D.
MAB_4230c fgd unknown Crystal structures of F420-dependent glucose-6-phosphate dehydrogenase FGD1 involved in the activation of the anti-tuberculosis drug candidate PA-824 reveal the basis of coenzyme and substrate binding 3B4Y Bashiri, G.,Squire, C.J.,Moreland, N.J.,Baker, E.N.
MMAR_0373 ptpB involved in signal transduction (via dephosphorylation). can dephosphorylated in vitro the phosphotyrosine residue of myelin basic protein (MBP) at ph 7.0. could be involved in virulence by interfering with phosphotyrosine-mediated signals in macrophages [catalytic activity: protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate]. Structural Basis for Selective Inhibition of Mycobacterium tuberculosis Protein Tyrosine Phosphatase PtpB. 2OZ5 Grundner, C.,Perrin, D.,Hooft van Huijsduijnen, R.,Swinnen, D.,Gonzalez, J.,Gee, C.L.,Wells, T.N.,Alber, T.
MMAR_5403 menG Crystal Structure of a Putative Methyltransferase from Mycobacterium tuberculosis: Misannotation of a Genome Clarified by Protein Structural Analysis 1NXJ Johnston, J.M.,Arcus, V.L.,Morton, C.J.,Parker, M.W.,Baker, E.N.
MSMEG_0435 MSMEG_0435 unknown Crystal Structure of Allphanate Hydrolase Complex from M. smegmatis, Msmeg0435-Msmeg0436 3MML Kaufmann, M.,Chernishof, I.,Shin, A.,Germano, D.,Sawaya, M.R.,Waldo, G.S.,Arbing, M.A.,Perry, J.,Eisenberg, D.
MSMEG_0436 MSMEG_0436 unknown Crystal Structure of Allphanate Hydrolase Complex from M. smegmatis, Msmeg0435-Msmeg0436 3MML Kaufmann, M.,Chernishof, I.,Shin, A.,Germano, D.,Sawaya, M.R.,Waldo, G.S.,Arbing, M.A.,Perry, J.,Eisenberg, D.
MSMEG_0620 MSMEG_0620 unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3Q4H Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
MSMEG_0621 MSMEG_0621 unknown Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. 3Q4H Arbing, M.A.,Chan, S.,Harris, L.,Kuo, E.,Zhou, T.T.,Ahn, C.J.,Nguyen, L.,He, Q.,Lu, J.,Menchavez, P.T.,Shin, A.,Holton, T.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
MSMEG_1843 ahcY unknown Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with substrate and inhibitors. 3DHY Reddy, M.C.,Kuppan, G.,Shetty, N.D.,Owen, J.L.,Ioerger, T.R.,Sacchettini, J.C.
MSMEG_2136 pgm unknown The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. 1RII Muller, P.,Sawaya, M.R.,Pashkov, I.,Chan, S.,Nguyen, C.,Wu, Y.,Perry, L.J.,Eisenberg, D.
MSMEG_2532 aroQ unknown Structural investigation of inhibitor designs targeting 3-dehydroquinate dehydratase from the shikimate pathway of Mycobacterium tuberculosis. 3N8K, 3N59 Dias, M.V.,Snee, W.C.,Bromfield, K.M.,Payne, R.J.,Palaninathan, S.K.,Ciulli, A.,Howard, N.I.,Abell, C.,Sacchettini, J.C.,Blundell, T.L.
MSMEG_2671 folA unknown Selective inhibitors for dihydrofolate reductase from mycobacterium tuberculosis 4M2X Jung, H.,Sacchettini, J.C.
MSMEG_3564 bfr unknown Mycobacterium tuberculosis bacterioferritin, BfrA 3UOI, 3UOF, 3QB9 McMath, L.M.,Goulding, C.W.
Mb0499 gpm1 unknown The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. 1RII Muller, P.,Sawaya, M.R.,Pashkov, I.,Chan, S.,Nguyen, C.,Wu, Y.,Perry, L.J.,Eisenberg, D.
Rv3800c pks13 Unknown Crystal Structure of Mtb Pks13 Thioesterase domain in complex with Compound 6. 7M7V, 6D8I, 6D8J, 5V3W, 5V3X, 5V3Y, 5V40, 5V40, 5V41, 5V42 Aggarwal, A.,Tang, S.,Sacchettini, J.C.
Rv1665 pks11 Unknown Crystal Structure of Mycobacterium tuberculosis PKS11 Reveals Intermediates in the Synthesis of Methyl-branched Alkylpyrones 4JAO, 4JAP, 4JAQ, 4JAR, 4JAT, 4JD3 Gokulan, K., Sacchettini, J.C.
Rv1484 inhA Unknown Crystal structure of wild-type InhA:NADH complex, a slow, tight Binding Inhibitor of Inha, the Enoyl-Acyl Carrier Protein Reductase from Mycobacterium Tuberculosis. 2H9I, 2NTJ, 2NTV, 2NV6, 3OEW, 3OEY, 3OF2, 4QXM, 5JFO, 1ZID, 1P44, 1P45, 2X23, 2X22, 5OIF, 5OIN, 5OIQ, 5OIC, 5OIO, 5OIL, 5OIM, 5OIT, 5OIR, 5OIS, 5OIP Molle, V., Gulten, G., Vilcheze, C., Veyron-Churlet, R., Zanella-Cleon, I.,Rozwarski, D.A., Sacchettini, J.C., Jacobs Jr, W.R., Kremer, L.,Kuo, M.R., Morbidoni, H.R., Alland, D., Sneddon, S.F., Gourlie, B.B., Staveski, M.M., Leonard, M., Gregory, J.S., Janjigian, A.D., Yee, C., Musser, J.M., Kreiswirth, B.,Fidock, D.A., Iwamoto, H., Perozzo, R.,Convery, M.A.,Luckner, S.R., Liu, N., am Ende, C.W., Tonge, P.J., Kisker, C.
Rv0211 pckA Unknown Crystal Structure of Mtb PEPCK in complex with GDP and metals 4WOU, 4WPT, 4WPU, 4WPV, 4WL8, 4WIE, 4WIU Kim, H.L., Sacchettini, J.C.
Rv1129c prpR Unknown Mycobacterium tuberculosis transcriptional regulator 6CYJ, 6CYY, 6CZ6, 6D2S Tang, S., Sacchettini, J.
Rv1570 bioD Unknown Crystal structure of dethiobiotin synthetase in Mycobacterium tuberculosis 3FGN, 3FMF, 3FMI, 3FPA Dey, S., Sacchettini, J.C.
Rv1568 bioA Unknown Crystal structure of Mycobacterium tuberculosis 7,8-diaminopelargonic acid synthase in complex with substrate analog sinefungin 3LV2, 3BV0 Dey, S., Sacchettini, J.C.
Rv0812 Rv0812 Unknown A hypothetical aminotransferase from Mycobacterium tuberculosis, apo form 6Q1R, 6Q1S Duan, L., Sacchettini, J.
Rv3722c Rv3722c Unknown Rv3722c in complex with glutamic acid,kynurenine,Rv3722c aminotransferase from Mycobacterium tuberculosis 6U78, 6U7A, 5C6U Mandyoli, L., Sacchettini, J.C., OSIPIUK, J., Hatzos-Skintges, C., Jedrzejczak, R., Babnigg, G., JOACHIMIAK, A.,
Rv3311 SatS chaperone The crystal structure of SatS c-terminal domain 6DNM, 6DRQ Hughes, R.C., Sacchettini, J.C.,
Rv1322a Rv1322a Unknown Crystal structure of methylmalonyl-CoA epimerase from Mycobacterium tuberculosis 6BU2 Hughes, R.C., Sacchettini, J.C.,
Rv0979A rpmF Unknown Cryo-EM structure of the 70S ribosome from Mycobacterium tuberculosis bound with Capreomycin 5V93, 7MSH, 7MSM, 7MSZ, 7MT2, 7MT3, 7MT7 Yang, K., Chang, J.-Y., Cui, Z., Li, X., Meng, R., Duan, L., Thongchol, J., Jakana, J., Huwe, C., Sacchettini, J., Zhang, J.
Rv3411c guaB2 Unknown Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the presence of TBK6 5UPU Kim, Y., Makowska-Grzyska, M., Maltseva, N., Mulligan, R., Gu, M., Sacchettini, J., Anderson, W.F., Joachimiak, A.
Rv0050 ponA1 Unknown Structure of the penicillin-binding protein PonA1 from Mycobacterium Tuberculosis 5CRF, 5CXW Filippova, E.V., Wawrzak, Z., Kiryukhina, O., Kieser, K., Endres, M., Rubin, E., Sacchettini, J.C., Joachimiak, A., Anderson, W.F.
Rv2535c pepQ Unknown Crystal structure of N-terminal domain of cytoplasmic peptidase PepQ from Mycobacterium tuberculosis H37Rv 5E2C Chang, C., Endres, L., Endres, M., Sacchettini, J.C., Joachimiak, A.
Rv0350 dnaK Unknown Crystal structure of molecular chaperone DnaK from Mycobacterium tuberculosis H37Rv 4RTF Filippova, E.V., Minasov, G., Kiryukhina, O., Endres, M., Babnigg, G., Rubin, E., Sacchettini, J., Joachimiak, A., Anderson, W.F.
Rv0379 secE2 Unknown Crystal structure of the calcium chelating immunodominant antigen, calcium dodecin (Rv0379),from Mycobacterium tuberculosis with a novel calcium-binding site 3ONR Arulandu, A., Sacchettini, J.C.
Rv0098 fcoT Unknown Structure of Mycobacterium tuberculosis Rv0098 2PFC Wang, F., Sacchettini, J.C.
Rv0967 csoR Unknown Crystal Structure of Cu(I) bound CsoR from Mycobacterium tuberculosis 2HH7 Sacchettini, J.C., Ramesh, A.
Rv1908c katG Unknown Crystal structure of the catalase-peroxidase (KatG) and S315T mutant from Mycobacterium tuberculosis 2CCA, 2CCD Yu, H., Sacchettini, J.C.
Rv0644c mmaA2 Unknown Structure of the cyclopropane synthase MmaA2 from Mycobacterium tuberculosis 1TPY Smith, C.V., Sacchettini, J.C.
Rv0129c fbpC2 Unknown Antigen 85C with octylthioglucoside in active site 1VA5 Ronning, D.R., Vissa, V., Besra, G.S., Belisle, J.T., Sacchettini, J.C.
Rv1293 lysA Unknown Mycobacterium diaminopimelate dicarboxylase (lysa) 1HKV, 1HKW Gokulan, K., Rupp, B., Pavelka Jr, M.S., Jacobs Jr, W.R., Sacchettini, J.C.
Rv3240c secA1 Unknown CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS 1NKT, 1NL3 Sharma, V., Arockiasamy, A., Ronning, D.R., Savva, C.G., Holzenburg, A., Braunstein, M., Jacobs Jr., W.R., Sacchettini, J.C.
Rv0006 gyrA Unknown GYRA INTEIN FROM MYCOBACTERIUM XENOPI 1AM2 Klabunde, T., Sharma, S., Sacchettini, J.C.
Rv0203 Rv0203 Unknown Discovery and characterization of a unique mycobacterial heme acquisition system. 3MAY Goulding, C.W., Chim, N.
Rv0202c mmpL11 Unknown The Structure and Interactions of Periplasmic Domains of Crucial MmpL Membrane Proteins from Mycobacterium tuberculosis. 4Y0L Torres, R., Chim, N., Goulding, C.W.
Rv1677 dsbF Unknown An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis. 3IOS, 6HF0, 6HEZ, 6HFW, 6HFV Chim, N., Goulding, C.W.
Rv3592 mhuD Unknown Crystal structure of MhuD R26S mutant with two Manganese protoporphyrin IX bound per active site, Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuD. Structure of aMycobacterium tuberculosisHeme-Degrading Protein, MhuD, Variant in Complex with Its Product. 6DS8, 6DS7, 3HX9, 4NL5, 6PLE Chao, A., Goulding, C.W.,Chim, N., Nguyen, T.Q., Iniguez, A., Morse, R.P.
Rv3607c folB Unknown Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme. 1NBU, 1Z9W Goulding, C.W., Apostol, M.I., Sawaya, M.R., Phillips, M., Parseghian, A., Eisenberg, D.
Rv2969c Rv2969c Unknown Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis. 4IHU Harmston, C.A., Goulding, C.W.
Rv2332 mez Unknown Structural and Molecular Dynamics of Mycobacterium tuberculosis Malic Enzyme, a Potential Anti-TB Drug Target. 6URF Cuthbert, B.J., Burley, K.H., Goulding, C.W., Mathews, E.I., Beste, D.J.
Rv2780 ald Unknown Drug target analysis by dye-ligand affinity chromatography. 4LMP Kim, H.-B., Hung, L.-W., Goulding, C.W., Terwilliger, T.C., Kim, C.-Y.
Rv3518c cyp142 Unknown Structural and Biochemical Characterization of Mycobacterium Tuberculosis Cyp142: Evidence for Multiple Cholesterol 27-Hydroxylase Activities in a Human Pathogen. 2XKR Driscoll, M., McLean, K.J., Levy, C.W., Lafite, P., Mast, N., Pikuleva, I.A., Rigby, S.E.J., Leys, D., Munro, A.W.
Rv2477c ettA Unknown Mtb 70SIC in complex with MtbEttA at Pre_R0 state. 7MSC, 7MU0 Cui, Z., Zhang, J.
MSMEG_6760 Unknown Crystal Structure of Protein Ms6760 from Mycobacterium smegmatis 3UID Bajaj, R.A., Miallau, L., Cascio, D., Arbing, M., Eisenberg, D., TB Structural Genomics Consortium (TBSGC)
Rv0301 vapC2 Unknown Rv0301 Rv0300 Toxin Antitoxin Complex from Mycobacterium tuberculosis 3H87 Min, A., Sawaya, M.R., Cascio, D., Eisenberg, D.
Rv3246c mtrA Unknown Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis 2GWR Friedland, N., Mack, T.R., Yu, M., Bursey, E.H., Hung, L.W., Stock, A.M., Waldo, G.S., Terwilliger, T.C.
Rv2632c Rv2632c Unknown Crystal Structure of Rv2632c 2FGG Yu, M., Bursey, E.H., Radhakannan, T., Segelke, B.W., Lekin, T., Toppani, D., Kim, C.Y., Kaviratne, T., Woodruff, T., Terwilliger, T.C., Hung, L.W., TB Structural Genomics Consortium (TBSGC)
Rv2593c ruvA Unknown RuvA from Mycobacterium tuberculosis 2H5X Prabu, J.R., Thamotharan, S., Khanduja, J.S., Alipio, E.Z., Kim, C.Y., Waldo, G.S., Terwilliger, T.C., Segelke, B., Lekin, T., Toppani, D., Hung, L.W., Yu, M., Bursey, E., Muniyappa, K., Chandra, N.R., Vijayan, M.
Rv1314c Rv1314c Unknown Crystal structure of a putative pduO-type ATP:cobalamin adenosyltransferase from Mycobacterium tuberculosis 2G2D Moon, J.H., Kaviratne, A., Yu, M., Bursey, E.H., Hung, L.-W., Lekin, T.P., Segelke, B.W., Terwilliger, T.C., Kim, C.-Y., TB Structural Genomics Consortium (TBSGC)
Rv2461c clpP1 Unknown Crystal structure of the atp-dependent clp protease proteolytic subunit 1 (clpp1) from mycobacterium tuberculosis 2CE3 Segelke, B., Kim, C.Y., Ortiz-Lombardia, M., Alzari, P.M., Lekin, T.
Rv3208A TB9.4 Unknown Crystal structure of the hexadecameric & octameric form of Rv3208A 7RUR, 7RUS Mandyoli, L., Sacchettini, J.C.