Structure of Escherichia coli pyruvate formate-lyase with pyruvate.
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.
Lehtiö
Lari
L
Institute of Biotechnology, University of Helsinki, PO Box 65, FIN-00014, Helsinki, Finland.
Leppänen
Veli-Matti
VM
Kozarich
John W
JW
Goldman
Adrian
A
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
D019289:Pyruvic Acid; D000123:Acetyltransferases; C022560:formate C-acetyltransferase