1q52
From Proteopedia
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|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK08321 PRK08321], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00378 ECH]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK08321 PRK08321], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00378 ECH]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q52 OCA], [http://www.ebi.ac.uk/pdbsum/1q52 PDBsum | + | |RELATEDENTRY=[[1dub|1DUB]], [[1ef8|1EF8]], [[1dci|1DCI]], [[1hnu|1HNU]], [[1nzy|1NZY]], [[1o8u|1O8U]], [[1q51|1Q51]] |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q52 OCA], [http://www.ebi.ac.uk/pdbsum/1q52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q52 RCSB]</span> | ||
}} | }} | ||
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[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:53 2008'' |
Revision as of 20:08, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Activity: | Naphthoate synthase, with EC number 4.1.3.36 | ||||||
| Domains: | PRK08321, ECH | ||||||
| Related: | 1DUB, 1EF8, 1DCI, 1HNU, 1NZY, 1O8U, 1Q51
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Mycobacterium tuberculosis MenB, a Key Enzyme in Vitamin K2 Biosynthesis
Overview
Bacterial enzymes of the menaquinone (Vitamin K2) pathway are potential drug targets because they lack human homologs. MenB, 1,4-dihydroxy-2-naphthoyl-CoA synthase, the fourth enzyme in the biosynthetic pathway leading from chorismate to menaquinone, catalyzes the conversion of O-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). Based on our interest in developing novel tuberculosis chemotherapeutics, we have solved the structures of MenB from Mycobacterium tuberculosis and its complex with acetoacetyl-coenzyme A at 1.8 and 2.3 A resolution, respectively. Like other members of the crotonase superfamily, MenB folds as an (alpha3)2 hexamer, but its fold is distinct in that the C terminus crosses the trimer-trimer interface, forming a flexible part of the active site within the opposing trimer. The highly conserved active site of MenB contains a deep pocket lined by Asp-192, Tyr-287, and hydrophobic residues. Mutagenesis shows that Asp-192 and Tyr-287 are essential for enzymatic catalysis. We postulate a catalytic mechanism in which MenB enables proton transfer within the substrate to yield an oxyanion as the initial step in catalysis. Knowledge of the active site geometry and characterization of the catalytic mechanism of MenB will aid in identifying new inhibitors for this potential drug target.
About this Structure
1Q52 is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.
Reference
Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis., Truglio JJ, Theis K, Feng Y, Gajda R, Machutta C, Tonge PJ, Kisker C, J Biol Chem. 2003 Oct 24;278(43):42352-60. Epub 2003 Aug 8. PMID:12909628
Page seeded by OCA on Sun Mar 30 23:08:53 2008
Categories: Mycobacterium tuberculosis h37rv | Naphthoate synthase | Single protein | Feng, Y. | Gajda, R. | Kisker, C. | Machutta, C. | TBSGC, TB Structural Genomics Consortium. | Theis, K. | Tonge, P J. | Truglio, J J. | Lyase | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc
