1umf
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(New page: 200px<br /><applet load="1umf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umf, resolution 2.25Å" /> '''crystal structure of...)
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Revision as of 02:07, 21 November 2007
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crystal structure of chorismate synthase
Overview
Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate, 3-phosphate to chorismate in the shikimate pathway, which represents an, attractive target for discovering antimicrobial agents and herbicides., Chorismate serves as a common precursor for the synthesis of aromatic, amino acids and many aromatic compounds in microorganisms and plants., Chorismate synthase requires reduced FMN as a cofactor but the catalyzed, reaction involves no net redox change. Here, we have determined the, crystal structure of chorismate synthase from Helicobacter pylori in both, FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer, possessing a novel "beta-alpha-beta sandwich fold". Highly conserved, regions, including several flexible loops, cluster together around the, bound FMN to form the active site. The unique FMN-binding site is formed, largely by a single subunit, with a small contribution from a neighboring, subunit. The isoalloxazine ring of the bound FMN is significantly, non-planar. Our structure illuminates the essential functional roles, played by the cofactor.
About this Structure
1UMF is a Single protein structure of sequence from Helicobacter pylori. Active as Chorismate synthase, with EC number 4.2.3.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights., Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW, J Mol Biol. 2004 Feb 27;336(4):903-15. PMID:15095868
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