新型 ATP 酶 RadD 来自大肠杆菌的晶体结构。

Crystal structure of a novel ATPase RadD from Escherichia coli.

机构信息

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, People's Republic of China.

College of Life Sciences, University of Chinese Academy of Sciences, Beijing, People's Republic of China.

出版信息

Proteins. 2019 Sep;87(9):791-795. doi: 10.1002/prot.25704. Epub 2019 May 9.

DOI:10.1002/prot.25704

PMID:31035307

Abstract

The helicase superfamily 2 (SF2) proteins are involved in essentially every step in DNA and RNA metabolism. The radD (yejH) gene, which belongs to SF2, plays an important role in DNA repair. The RadD protein includes all seven conserved SF2 motifs and has shown ATPase activity. Here, we first reported the structure of RadD from Escherichia coli containing two RecA-like domains, a zinc finger motif, and a C-terminal domain. Based on the structure of RadD and other SF2 proteins, we then built a model of the RedD-ATP complex.

摘要

解旋酶超家族 2（SF2）蛋白参与 DNA 和 RNA 代谢的几乎每一个步骤。属于 SF2 的 radD（yejH）基因在 DNA 修复中起着重要作用。RadD 蛋白包含所有七个保守的 SF2 基序，并表现出 ATP 酶活性。在这里，我们首次报道了含有两个 RecA 样结构域、一个锌指结构域和一个 C 末端结构域的大肠杆菌 RadD 结构。基于 RadD 和其他 SF2 蛋白的结构，我们随后构建了 RedD-ATP 复合物的模型。