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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期刊:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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分类:
生物学
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生物物理学
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生物物理、生物化学与分子生物学
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引用:
ChinaXiv:201605.01738
(或此版本
ChinaXiv:201605.01738V1)
DOI:10.12074/201605.01738V1
CSTR:32003.36.ChinaXiv.201605.01738.V1
- 推荐引用方式:
He, Zheng,Gao, Yuan,Li, Xuemei,Zhang, Xuejun C.,He, Zheng,Dong, Jing,Ke, Yuehua,Chen, Zeliang.(2016).Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus.中国生物工程预印本出版平台.[ChinaXiv:201605.01738]
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