1UM0

Crystal structure of chorismate synthase complexed with FMN

Summary for 1UM0

• Entry DOI: 10.2210/pdb1um0/pdb
• Descriptor: Chorismate synthase, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: beta-alpha-beta sandwich fold, lyase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 4
• Total formula weight: 162445.14

Authors

Ahn, H.J.,Yoon, H.J.,Lee, B.,Suh, S.W. (deposition date: 2003-09-18, 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

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: 15095868
DOI: 10.1016/j.jmb.2003.12.072

Experimental method

X-RAY DIFFRACTION (1.95 Å)