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. doi: 10.1016/j.jmb.2006.04.060. Epub 2006 May 11.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Binding Sites
  • Brucella suis / enzymology*
  • Escherichia coli / metabolism
  • Helicobacter pylori / metabolism
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Plasmids / metabolism
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Adenosine Triphosphatases

Associated data

  • PDB/2GZA