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Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus

文献类型： 外文期刊

作者： He, Zheng 1 ; Gao, Yuan 1 ; Dong, Jing 3 ; Ke, Yuehua 4 ; Li, Xuemei 1 ; Chen, Zeliang 4 ; Zhang, Xuejun C. 1 ;

作者机构： 1.Chinese Acad Sci, Natl Ctr Prot Sci Beijing, Inst Biophys, Natl Lab Macromol, Beijing 100101, Peoples R China

2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China

3.Chinese Acad Fishery Sci, Yangtze River Fisheris Res Inst, Wuhan 430224, Peoples R China

4.Acad Mil Med Sci, Inst Dis Control & Prevent, Beijing 100071, Peoples R China

关键词： Brucella abortus;Cyclic nucleotide binding (CNB) domain;Crystal structure

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

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收录情况： SCI

摘要： The cyclic nucleotide-binding (CNB)-like protein (CNB-L) from Brucella abortus shares sequence homology with CNB domain-containing proteins. We determined the crystal structure of CNB-L at 2.0 angstrom resolution in the absence of its C-terminal helix and nucleotide. The 3D structure of CNB-L is in a twofold symmetric form. Each protomer shows high structure similarity to that of cGMP-binding domain-containing proteins, and likely mimics their nucleotide-free conformation. A key residue, Glu17, mediates the dimerization and prevents binding of cNMP to the canonical ligand-pocket. The structurally observed dimer of CNB-L is stable in solution, and thus is likely to be biologically relevant. (C) 2015 Elsevier Inc. All rights reserved.

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