ยท S.Hare, R. Bayliss, C. Baron, and G.
Waksman
A large domain swap in the VirB11 ATPase
of Brucella suis
leaves the hexameric assembly intact
Journal of Molecular Biology. 360:56-66. (2006)
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 (NTD) and C-terminal (CTD) 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.