1um0: Difference between revisions

Revision as of 03:42, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1um0.png

Template:STRUCTURE 1um0

Crystal structure of chorismate synthase complexed with FMNCrystal structure of chorismate synthase complexed with FMN

Template:ABSTRACT PUBMED 15095868

About this StructureAbout this Structure

1UM0 is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 03:42:45 2008

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OCA

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-'''Crystal structure of chorismate synthase complexed with FMN'''
+===Crystal structure of chorismate synthase complexed with FMN===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15095868}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15095868 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15095868}}
 ==About this Structure==
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 [[Category: Yoon, H J.]]
 [[Category: Beta-alpha-beta sandwich fold]]
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