1mzo | pdb_00001mzo

Crystal structure of pyruvate formate-lyase with pyruvate

spinqualitylabelsall models 1mzo, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mzo is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PGE, PYR Activity: Formate C-acetyltransferase, with EC number 2.3.1.54 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 The structure of inactive pyruvate formate-lyase in complex with a natural substrate, pyruvate, was solved at 2.7 A resolution. Both active sites of the homodimeric enzyme are occupied by pyruvate; additional binding sites were not found. Pyruvate was found in a cleft close to the active-site cysteines 418 and 419, with the carboxyl group in contact with arginines 176 and 435 and the methyl group within van der Waals distance of Phe327. It is believed that the binding site of pyruvate is not the position of pyruvate as the reaction initiates, as conformational changes occur during activation of the enzyme. Structure of Escherichia coli pyruvate formate-lyase with pyruvate.,Lehtio L, Leppanen VM, Kozarich JW, Goldman A Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2209-12. Epub 2002, Nov 23. PMID:12454503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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