1bvr: Difference between revisions

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[[Image:1bvr.gif|left|200px]]
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[[Image:1bvr.png|left|200px]]


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{{STRUCTURE_1bvr|  PDB=1bvr  |  SCENE=  }}  
{{STRUCTURE_1bvr|  PDB=1bvr  |  SCENE=  }}  


'''M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE'''
===M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE===




==Overview==
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Enoyl-ACP reductases participate in fatty acid biosynthesis by utilizing NADH to reduce the trans double bond between positions C2 and C3 of a fatty acyl chain linked to the acyl carrier protein. The enoyl-ACP reductase from Mycobacterium tuberculosis, known as InhA, is a member of an unusual FAS-II system that prefers longer chain fatty acyl substrates for the purpose of synthesizing mycolic acids, a major component of mycobacterial cell walls. The crystal structure of InhA in complex with NAD+ and a C16 fatty acyl substrate, trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester, reveals that the substrate binds in a general "U-shaped" conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore could help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates.
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{{ABSTRACT_PUBMED_10336454}}


==About this Structure==
==About this Structure==
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[[Category: Tb structural genomics consortium]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Tbsgc]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:00:48 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:47:38 2008''

Revision as of 16:47, 30 June 2008

File:1bvr.png

Template:STRUCTURE 1bvr

M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE

Template:ABSTRACT PUBMED 10336454

About this Structure

1BVR is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate., Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC, J Biol Chem. 1999 May 28;274(22):15582-9. PMID:10336454

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