Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10749168 | Biochemical and Biophysical Research Communications | 2015 | 6 Pages |
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 2.0Â Ã
resolution in the absence of its C-terminal helix and nucleotide. The 3D structure of CNB-L is in a two-fold 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.
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Biochemistry
Authors
Zheng He, Yuan Gao, Jing Dong, Yuehua Ke, Xuemei Li, Zeliang Chen, Xuejun C. Zhang,