title: Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.
abstract: We have determined the three-dimensional crystal structure of the protein encoded by the open reading frame YFL030w from Saccharomyces cerevisiae to a resolution of 2.6 A using single wavelength anomalous diffraction. YFL030w is a 385 amino-acid protein with sequence similarity to the aminotransferase family. The structure of the protein reveals a homodimer adopting the fold-type I of pyridoxal 5'-phosphate (PLP)-dependent aminotransferases. The PLP co-factor is covalently bound to the active site in the crystal structure. The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase (EC 2.6.1.44), an enzyme involved in the hereditary kidney stone disease primary hyperoxaluria type 1. In this paper we show that YFL030w codes for an alanine:glyoxylate aminotransferase, highly specific for its amino donor and acceptor substrates.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-UPR 9063) Bât. 34, 1, avenue de la Terrasse, 91198 Gif sur Yvette cedex, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Meyer
authors.forename: Dominique
authors.initials: D
authors.lastname: Liger
authors.forename: Nicolas
authors.initials: N
authors.lastname: Leulliot
authors.forename: Sophie
authors.initials: S
authors.lastname: Quevillon-Cheruel
authors.forename: Cong-Zhao
authors.initials: CZ
authors.lastname: Zhou
authors.forename: Franck
authors.initials: F
authors.lastname: Borel
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Ferrer
authors.forename: Anne
authors.initials: A
authors.lastname: Poupon
authors.forename: Joël
authors.initials: J
authors.lastname: Janin
authors.forename: Herman
authors.initials: H
authors.lastname: van Tilbeurgh
mesh_terms: D002236:Carbohydrate Conformation; D018360:Crystallography, X-Ray; D007700:Kinetics; D008958:Models, Molecular; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry* / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D000637:Transaminases; C510187:AGX1 protein, S cerevisiae