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


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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Recommended references: 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.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS.[ChinaXiv:201605.01738] (Click&Copy)
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[V1] 2016-05-15 13:34:23 chinaXiv:201605.01738V1 Download
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