5D1I

Structure of Cyclic nucleotide-binding-like protein from Brucella abortus bv. 1 str. 9-941

Summary for 5D1I

• Entry DOI: 10.2210/pdb5d1i/pdb
• Descriptor: Cyclic nucleotide-binding protein (2 entities in total)
• Functional Keywords: beta barrel, unknown function
• Biological source: Brucella abortus biovar 1
• Total number of polymer chains: 2
• Total formula weight: 28910.42

Authors

He, Z.,Dong, J.,Li, X.,Gao, Y. (deposition date: 2015-08-04, release date: 2015-09-09, Last modification date: 2024-10-16)

Primary citation

He, Z.,Gao, Y.,Dong, J.,Ke, Y.,Li, X.,Chen, Z.,Zhang, X.C.
Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus
Biochem.Biophys.Res.Commun., 468:647-652, 2015

PubMed 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 Å 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.

PubMed: 26549229
DOI: 10.1016/j.bbrc.2015.11.005

Experimental method

X-RAY DIFFRACTION (2 Å)