title: A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.
abstract: VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits.
authors.affiliation: School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
authors.forename: Stephen
authors.initials: S
authors.lastname: Hare
authors.forename: Richard
authors.initials: R
authors.lastname: Bayliss
authors.forename: Christian
authors.initials: C
authors.lastname: Baron
authors.forename: Gabriel
authors.initials: G
authors.lastname: Waksman
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D001665:Binding Sites; D041021:Brucella suis / Q000201:enzymology*; D004926:Escherichia coli / Q000378:metabolism; D016480:Helicobacter pylori / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D000251:Adenosine Triphosphatases