1uzn
From Proteopedia
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| - | [[Image:1uzn.gif|left|200px]]<br /><applet load="1uzn" size=" | + | [[Image:1uzn.gif|left|200px]]<br /><applet load="1uzn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uzn, resolution 1.91Å" /> | caption="1uzn, resolution 1.91Å" /> | ||
'''MABA FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | '''MABA FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UZN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CS and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] Known structural/functional Site: <scene name='pdbsite=AC1:Nap Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1UZN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=CS:'>CS</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] Known structural/functional Site: <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:13:06 2008'' |
Revision as of 08:13, 3 February 2008
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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
1UZN is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Known structural/functional Site: . 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 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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