Meyer Philippe, Liger Dominique, Leulliot Nicolas, Quevillon-Cheruel Sophie, Zhou Cong-Zhao, Borel Franck, Ferrer Jean-Luc, Poupon Anne, Janin Joël, van Tilbeurgh Herman
Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-UPR 9063) Bât. 34, 1, avenue de la Terrasse, 91198 Gif sur Yvette cedex, France.
Biochimie. 2005 Dec;87(12):1041-7. doi: 10.1016/j.biochi.2005.09.001. Epub 2005 Oct 5.
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.
我们利用单波长反常衍射法，将酿酒酵母开放阅读框YFL030w编码的蛋白质的三维晶体结构解析到了2.6埃的分辨率。YFL030w是一种含有385个氨基酸的蛋白质，其序列与转氨酶家族相似。该蛋白质的结构显示它是一个同型二聚体，采用了依赖于磷酸吡哆醛（PLP）的转氨酶的折叠类型I。在晶体结构中，PLP辅因子与活性位点共价结合。该蛋白质与人类丙氨酸：乙醛酸转氨酶（EC 2.6.1.44）在结构上非常相似，后者是一种参与遗传性肾结石疾病——I型原发性高草酸尿症的酶。在本文中，我们表明YFL030w编码一种丙氨酸：乙醛酸转氨酶，它对其氨基供体和受体底物具有高度特异性。
