1pkv

The N-terminal domain of riboflavin synthase in complex with riboflavin

spinqualitylabelsall models 1pkv, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pkv is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RBF Related: 1hze, 1i8d, 1kzl Gene: RIBE OR RIBC OR B1662 OR SF1690 (Escherichia coli) Activity: Riboflavin synthase, with EC number 2.5.1.9 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RISA_ECOLI] Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N-terminal segment (residues 1-87) and the C-terminal segment (residues 98-187) form beta-barrels with similar fold and a high degree of sequence similarity. A recombinant peptide comprising amino acid residues 1-97 forms a dimer, which binds riboflavin with high affinity. Here, we report the structure of this construct in complex with riboflavin at 2.6A resolution. It is demonstrated that the complex can serve as a model for ligand-binding in the native enzyme. The structure and riboflavin-binding mode is in excellent agreement with structural information obtained from the native enzyme from Escherichia coli and riboflavin synthase from Schizosaccharomyces pombe. The implications for the binding specificity and the regiospecificity of the catalyzed reaction are discussed. The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution.,Meining W, Eberhardt S, Bacher A, Ladenstein R J Mol Biol. 2003 Aug 29;331(5):1053-63. PMID:12927541 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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