Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.
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.
Meyer
Philippe
P
Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-UPR 9063) Bât. 34, 1, avenue de la Terrasse, 91198 Gif sur Yvette cedex, France.
Liger
Dominique
D
Leulliot
Nicolas
N
Quevillon-Cheruel
Sophie
S
Zhou
Cong-Zhao
CZ
Borel
Franck
F
Ferrer
Jean-Luc
JL
Poupon
Anne
A
Janin
Joël
J
van Tilbeurgh
Herman
H
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
D029701:Saccharomyces cerevisiae Proteins; D000637:Transaminases; C510187:AGX1 protein, S cerevisiae