Structural highlights
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 PubMedWe 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. Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.,Meyer P, Liger D, Leulliot N, Quevillon-Cheruel S, Zhou CZ, Borel F, Ferrer JL, Poupon A, Janin J, van Tilbeurgh H Biochimie. 2005 Dec;87(12):1041-7. Epub 2005 Oct 5. PMID:16226833[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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