5d1i

Publication Abstract from PubMed

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 A 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.

Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus.,He Z, Gao Y, Dong J, Ke Y, Li X, Chen Z, Zhang XC Biochem Biophys Res Commun. 2015 Dec 25;468(4):647-52. doi:, 10.1016/j.bbrc.2015.11.005. Epub 2015 Nov 6. PMID:26549229^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.