1uzm
From Proteopedia
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[[Image:1uzm.gif|left|200px]] | [[Image:1uzm.gif|left|200px]] | ||
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'''MABA FROM MYCOBACTERIUM TUBERCULOSIS''' | '''MABA FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
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==Reference== | ==Reference== | ||
Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis., Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A, J Mol Biol. 2002 Jul 5;320(2):249-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12079383 12079383] | Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis., Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A, J Mol Biol. 2002 Jul 5;320(2):249-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12079383 12079383] | ||
| - | [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Labesse, G.]] | [[Category: Labesse, G.]] | ||
[[Category: Quemard, A.]] | [[Category: Quemard, A.]] | ||
| - | [[Category: | + | [[Category: Beta-ketoacyl reductase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:54:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:54, 3 May 2008
MABA FROM MYCOBACTERIUM TUBERCULOSIS
Overview
The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are major and specific long-chain fatty acids of the cell envelope of Mycobacterium tuberculosis and other mycobacteria, including Mycobacterium smegmatis. The protein MabA, also named FabG1, has been shown recently to be part of FAS-II and to catalyse the NADPH-specific reduction of long chain beta-ketoacyl derivatives. This activity corresponds to the second step of an FAS-II elongation round. FAS-II is inhibited by the antituberculous drug isoniazid through the inhibition of the 2-trans-enoyl-acyl carrier protein reductase InhA. Thus, the other enzymes making up this enzymatic complex represent potential targets for designing new antituberculous drugs. The crystal structure of the apo-form MabA was solved to 2.03 A resolution by molecular replacement. MabA is tetrameric and shares the conserved fold of the short-chain dehydrogenases/reductases (SDRs). However, it exhibits some significant local rearrangements of the active-site loops in the absence of a cofactor, particularly the beta5-alpha5 region carrying the unique tryptophan residue, in agreement with previous fluorescence spectroscopy data. A similar conformation has been observed in the beta-ketoacyl reductase from Escherichia coli and the distantly related dehydratase. The distinctive enzymatic and structural properties of MabA are discussed in view of its crystal structure and that of related enzymes.
About this Structure
1UZM is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis., Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A, J Mol Biol. 2002 Jul 5;320(2):249-61. PMID:12079383 Page seeded by OCA on Sat May 3 11:54:35 2008
