苯丙氨酰 - tRNA合成酶和生物素合成酶非催化结构域的结构相似性。
Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases.
作者信息
Safro M, Mosyak L
机构信息
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
出版信息
Protein Sci. 1995 Nov;4(11):2429-32. doi: 10.1002/pro.5560041122.
Abstract
Detailed comparison between the structures of the Escherichia coli biotin synthetase/repressor protein (BirA) and the recently solved Thermus thermophilus phenylalanyl-tRNA synthetase (PheRS) reveals significant similarities outside their respective catalytic domains. These comprise a DNA-binding alpha+beta domain and an Src-homology 3 (SH3)-like domain that were observed in both enzymes. This similarity provides a novel example in which all domains of one multidomain protein appear to be constituents of the other multidomain protein and supports a concept of a common ancestor for two different synthetase families.
摘要
大肠杆菌生物素合成酶/阻遏蛋白（BirA）与最近解析出结构的嗜热栖热菌苯丙氨酰 - tRNA合成酶（PheRS）之间的详细比较显示，在它们各自的催化结构域之外存在显著相似性。这些相似性包括在两种酶中均观察到的一个DNA结合α + β结构域和一个类Src同源3（SH3）结构域。这种相似性提供了一个新的例子，即一个多结构域蛋白的所有结构域似乎都是另一个多结构域蛋白的组成部分，并支持了两个不同合成酶家族拥有共同祖先的概念。
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