1UMF
crystal structure of chorismate synthase
Summary for 1UMF
| Entry DOI | 10.2210/pdb1umf/pdb |
| Related | 1UM0 |
| Descriptor | Chorismate synthase (2 entities in total) |
| Functional Keywords | beta-alpha-beta sandwich fold, lyase |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 4 |
| Total formula weight | 160619.76 |
| Authors | Ahn, H.J.,Yoon, H.J.,Lee, B.,Suh, S.W. (deposition date: 2003-09-30, release date: 2004-06-01, Last modification date: 2023-12-27) |
| Primary citation | Ahn, H.J.,Yoon, H.J.,Lee, B.,Suh, S.W. Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights J.Mol.Biol., 336:903-915, 2004 Cited by PubMed 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. PubMed: 15095868DOI: 10.1016/j.jmb.2003.12.072 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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