Format

Send to

Choose Destination
J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11.

A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.

Author information

1
School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.

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.

PMID:
16730027
DOI:
10.1016/j.jmb.2006.04.060
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center