title: Crystallographic analysis of Bacillus subtilis CsaA.
abstract: Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal structure of CsaA from the Gram-negative eubacterium Thermus thermophilus (TtCsaA) and provide a direct structural basis for the interpretation of previously available biochemical data on BsCsaA. The sequence and structure of the proposed substrate-binding pocket are analyzed and discussed. A comparison with the TtCsaA structure reveals a different pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and discussed.
authors: Department of Molecular Biology and Biochemistry, Simon Fraser University, South Science Building, 8888 University Drive, Burnaby, British Columbia V5A 1S6, Canada.
authors: Yuliya A
authors: YA
authors: Shapova
authors: Mark
authors: M
authors: Paetzel
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; C077891:CsaA protein, Bacillus subtilis