A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact |
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| Authors: | Hare Stephen Bayliss Richard Baron Christian Waksman Gabriel |
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| Institution: | School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK. |
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| 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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| Keywords: | T4SS the type IV secretion system CTD C-terminal domain NTD N-terminal domain NBS nucleotide-binding site |
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