2vb9

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{{STRUCTURE_2vb9| PDB=2vb9 | SCENE= }}
{{STRUCTURE_2vb9| PDB=2vb9 | SCENE= }}
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'''BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI, APO STRUCTURE'''
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===BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI, APO STRUCTURE===
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==Overview==
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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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{{ABSTRACT_PUBMED_18084068}}
==About this Structure==
==About this Structure==
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[[Category: Lipid synthesis]]
[[Category: Lipid synthesis]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:32:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:25:55 2008''

Revision as of 10:26, 27 July 2008

Image:2vb9.png

Template:STRUCTURE 2vb9

BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI, APO STRUCTURE

Template:ABSTRACT PUBMED 18084068

About this Structure

2VB9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Sun Jul 27 13:25:55 2008

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