title: Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus.
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.
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science- Beijing, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
authors.forename: Zheng
authors.initials: Z
authors.lastname: He
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science- Beijing, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.
authors.forename: Yuan
authors.initials: Y
authors.lastname: Gao
authors.affiliation: Yangtze River Fisheris Research Institute, Chinese Academy of Fishery Sciences, Wuhan, 430224, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Dong
authors.affiliation: Institute of Disease Control and Prevention, Academy of Military Medical Sciences, Beijing, 100071, China.
authors.forename: Yuehua
authors.initials: Y
authors.lastname: Ke
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science- Beijing, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.
authors.forename: Xuemei
authors.initials: X
authors.lastname: Li
authors.affiliation: Institute of Disease Control and Prevention, Academy of Military Medical Sciences, Beijing, 100071, China.
authors.forename: Zeliang
authors.initials: Z
authors.lastname: Chen
authors.affiliation: National Laboratory of Macromolecules, National Center of Protein Science- Beijing, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China. Electronic address: zhangc@ibp.ac.cn.
authors.forename: Xuejun C
authors.initials: XC
authors.lastname: Zhang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D002003:Brucella abortus / Q000378:metabolism*; D019281:Dimerization; D005973:Glutamine / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D009712:Nucleotides, Cyclic / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; D009712:Nucleotides, Cyclic; D005973:Glutamine
keywords: Brucella abortus; Crystal structure; Cyclic nucleotide binding (CNB) domain