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|Title:||A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.|
|Citation:||J MOL BIOL, 2006, 360 (1), pp. 56-66|
|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.|
|Appears in Collections:||Published Articles, Dept. of Biochemistry|
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