Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10804476 | Biochimie | 2005 | 7 Pages |
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 2.6Â Ã
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 5â²-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.
Keywords
PLPSingle wavelength anomalous diffractionSe-MetpH1Ni-NTAPDBIPTGAlanine:glyoxylate aminotransferaseEDTAEthylenediaminetetraacetic acidSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisisopropyl β-D-1-thiogalactopyranosideTris(hydroxymethyl)aminomethane hydrochlorideTris–HClCrystal structureSelenomethionineSADPrimary hyperoxaluria type 1polymerase chain reactionPCRProtein Data Bankpolyethylene glycol monomethyl etherpyridoxal 5′-phosphate
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Authors
Philippe Meyer, Dominique Liger, Nicolas Leulliot, Sophie Quevillon-Cheruel, Cong-Zhao Zhou, Franck Borel, Jean-Luc Ferrer, Anne Poupon, Joël Janin, Herman van Tilbeurgh,