Structural highlights
Function
VIRBB_BRUSU The VirB system could be required for the establishment of the replication niche in the host.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.,Hare S, Bayliss R, Baron C, Waksman G J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11. PMID:16730027[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hare S, Bayliss R, Baron C, Waksman G. A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact. J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11. PMID:16730027 doi:10.1016/j.jmb.2006.04.060
