Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights |
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Authors: | Ahn Hyung Jun Yoon Hye-Jin Lee Byung Suh Se Won |
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Institution: | Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-0742, South Korea. |
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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 "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. |
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Keywords: | aroC chorismate synthase FMN-binding protein Helicobacter pylori shikimate pathway |
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