title: Structure of Escherichia coli pyruvate formate-lyase with pyruvate.
abstract: 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.
authors.affiliation: Institute of Biotechnology, University of Helsinki, PO Box 65, FIN-00014, Helsinki, Finland.
authors.forename: Lari
authors.initials: L
authors.lastname: Lehtiö
authors.forename: Veli-Matti
authors.initials: VM
authors.lastname: Leppänen
authors.forename: John W
authors.initials: JW
authors.lastname: Kozarich
authors.forename: Adrian
authors.initials: A
authors.lastname: Goldman
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D019289:Pyruvic Acid / Q000737:chemistry* / Q000378:metabolism
chemical_list: D019289:Pyruvic Acid; D000123:Acetyltransferases; C022560:formate C-acetyltransferase