STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO-ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS
STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO-ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS
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DOI：
10.1126/science.3898365
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发表时间：
1985-01-01
期刊：
影响因子：
56.9
通讯作者：
JURNAK, F
中科院分区：
文献类型：
--
作者：
JURNAK, F
对胰蛋白酶修饰形式的大肠杆菌延伸因子Tu进行的2.7埃分辨率X射线衍射分析表明，GDP结合结构域具有与其他核苷酸结合蛋白相似的结构。 GDP 配体位于 β 片层的 COOH 末端，并通过 Mg2+ 离子盐桥与蛋白质连接。鸟嘌呤环的位置很不寻常；嘌呤环位于结构域的外边缘，不在疏水袋的深处。从Pro10到Arg44以及从Gly59到Glu190的氨基酸已通过计算机图形技术分配给电子密度，所得模型与所有已知的生化数据一致。结构分析表明，与原癌基因蛋白家族同源的四个氨基酸序列区域（称为p21）位于GDP结合位点附近，并且蛋白质共享的大多数不变氨基酸直接与GDP配体相互作用。
A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of theEscherichia colielongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the β sheet and is linked to the protein via a Mg2+ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10to Arg44and from Gly59to Glu190have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family ofrasoncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.