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

Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology submitted time 2016-05-15

He, Zheng Gao, Yuan Li, Xuemei Zhang, Xuejun C. He, Zheng Dong, Jing Ke, Yuehua Chen, Zeliang

Abstract： 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.

Peer Review Status:Awaiting Review

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