Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2189579 | Journal of Molecular Biology | 2006 | 11 Pages |
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.
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Authors
Stephen Hare, Richard Bayliss, Christian Baron, Gabriel Waksman,