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Title: A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.
Authors: Hare, S
Bayliss, R
Baron, C
Waksman, G
First Published: 30-Jun-2006
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.
DOI Link: 10.1016/j.jmb.2006.04.060
ISSN: 0022-2836
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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