Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein |
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Authors: | Meyer Philippe Liger Dominique Leulliot Nicolas Quevillon-Cheruel Sophie Zhou Cong-Zhao Borel Franck Ferrer Jean-Luc Poupon Anne Janin Joël van Tilbeurgh Herman |
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Institution: | Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-UPR 9063) Bat. 34, 1, avenue de la Terrasse, 91198 Gif sur Yvette cedex, France. |
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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. |
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