Title of article :
Crystal Structure of Chorismate Synthase: A Novel FMN-binding Protein Fold and Functional Insights
Author/Authors :
Hyung Jun Ahn، نويسنده , , Hye-Jin Yoon، نويسنده , , Byung-Il Lee، نويسنده , , Se Won Suh، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2004
Pages :
13
From page :
903
To page :
915
Abstract :
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 “β-α-β 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.
Keywords :
FMN-binding protein , shikimate pathway , Helicobacter pylori , aroC , chorismate synthase
Journal title :
Journal of Molecular Biology
Serial Year :
2004
Journal title :
Journal of Molecular Biology
Record number :
1243412
Link To Document :
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