PDBsum entry 5d1i

Unknown function

PDB id: 5d1i

Contents

Protein chains

117 a.a.

Waters ×171

PDB id:

5d1i

Name:

Unknown function

Title:

Structure of cyclic nucleotide-binding-like protein from brucella abortus bv. 1 str. 9-941

Structure:

Cyclic nucleotide-binding protein. Chain: a, b. Fragment: unp residues 1-123. Engineered: yes

Source:

Brucella abortus biovar 1. Organism_taxid: 262698. Strain: 9-941. Gene: bruab1_1980. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.188 R-free: 0.233

Authors:

Z.He,J.Dong,X.Li,Y.Gao

Key ref:

Z.He et al. (2015). Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus. Biochem Biophys Res Commun, 468, 647-652. PubMed id: 26549229 DOI: 10.1016/j.bbrc.2015.11.005

Date:

04-Aug-15 Release date: 09-Sep-15

Protein chains

Q57AQ0  (Q57AQ0_BRUAB) -  Cyclic nucleotide-binding protein from Brucella abortus biovar 1 (strain 9-941)

Seq: 153 a.a.

Struc: 117 a.a.

DOI no: 10.1016/j.bbrc.2015.11.005

Biochem Biophys Res Commun 468:647-652 (2015)

PubMed id: 26549229

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

Z.He, Y.Gao, J.Dong, Y.Ke, X.Li, Z.Chen, X.C.Zhang.

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.