A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.
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.
Hare
Stephen
S
School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
Bayliss
Richard
R
Baron
Christian
C
Waksman
Gabriel
G
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
D001426:Bacterial Proteins; D000251:Adenosine Triphosphatases