Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli
Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli
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DOI：
10.1016/j.jsb.2011.01.008
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发表时间：
2011-05-01
影响因子：
3
通讯作者：
Jiang, Tao
中科院分区：
文献类型：
--
作者：
Gui, Wen-Jun;Qu, Qian-Hui;Jiang, Tao
小MutS相关（Smr）结构域（MutS 2的C-末端核酸内切酶结构域）的序列同源物也作为独立的蛋白质存在。在这项研究中，我们报告了YdaL（39-175）的蛋白水解片段的晶体结构。来自大肠杆菌的独立Smr蛋白在该结构中，残基86-170组装成经典Smr核心结构域，并被具有α/β/α折叠的N-末端延伸（残基40-85）包围。序列比对表明，N-末端延伸是保守的一些独立的Smr蛋白，这表明Smr结构域之间的结构多样性。我们还发现，截短的YdaL（39-175）蛋白的DNA结合亲和力和核酸内切酶活性略低于全长YdaL（1-187），表明残基1-38可能参与DNA结合。(C)2011 Elsevier Inc. All rights reserved.
Sequence homologs of the small MutS-related (Smr) domain, the C-terminal endonuclease domain of MutS2, also exist as stand-alone proteins. In this study, we report the crystal structure of a proteolyzed fragment of YdaL(YdaL(39-175)). a stand-alone Smr protein from Escherichia colt In this structure, residues 86-170 assemble into a classical Smr core domain and are embraced by an N-terminal extension (residues 40-85) with an alpha/beta/ a fold. Sequence alignment indicates that the N-terminal extension is conserved among a number of stand-alone Smr proteins, suggesting structural diversity among Smr domains. We also discovered that the DNA binding affinity and endonuclease activity of the truncated YdaL(39-175) protein were slightly lower than those of full-length YdaL(1-187), suggesting that residues 1-38 may be involved in DNA binding. (C) 2011 Elsevier Inc. All rights reserved.