University of Sussex
Browse

File(s) not publicly available

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

journal contribution
posted on 2023-06-09, 08:02 authored by Stephen Hare, Richard Bayliss, Christian Baron, Gabriel Waksman
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.

History

Publication status

  • Published

Journal

Journal of Molecular Biology

ISSN

0022-2836

Publisher

Elsevier

Issue

1

Volume

360

Page range

56-66

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2017-09-21

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC