2vb8: Difference between revisions

Revision as of 20:22, 28 July 2008

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File:2vb8.png

Template:STRUCTURE 2vb8

BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCINBETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCIN

Template:ABSTRACT PUBMED 18084068

About this StructureAbout this Structure

2VB8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis., Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1208-16. Epub 2007, Nov 16. PMID:18084068

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCIN'''
+===BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCIN===
-==Overview==
+<!--
-Fatty-acid synthesis in bacteria is of great interest as a target for the discovery of antibacterial compounds. The addition of a new acetyl moiety to the growing fatty-acid chain, an essential step in this process, is catalyzed by beta-ketoacyl-ACP synthase (KAS). It is inhibited by natural antibiotics such as cerulenin and thiolactomycin; however, these lack the requirements for optimal drug development. Structure-based biophysical screening revealed a novel synthetic small molecule, 2-phenylamino-4-methyl-5-acetylthiazole, that binds to Escherichia coli KAS I with a binding constant of 25 microM as determined by fluorescence titration. A 1.35 A crystal structure of its complex with its target reveals noncovalent interactions with the active-site Cys163 and hydrophobic residues of the fatty-acid binding pocket. The active site is accessible through an open conformation of the Phe392 side chain and no conformational changes are induced at the active site upon ligand binding. This represents a novel binding mode that differs from thiolactomycin or cerulenin interaction. The structural information on the protein-ligand interaction offers strategies for further optimization of this low-molecular-weight compound.
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 ==About this Structure==
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 [[Category: Thiolactomycin]]
 [[Category: Transferase]]
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