Motion in VirB11 ATPase (HP0525) [virb11]

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Classification [S-a-2]


From the abstract to Savvides et al. (EMBO J.22:1969-80): "In the absence of nucleotide, the N-terminal domains exhibit a collection of rigid-body conformations. Nucleotide binding 'locks' the hexamer into a symmetric and compact structure. We propose that VirB11s use the mechanical leverage generated by such nucleotide-dependent conformational changes to facilitate the export of substrates or the assembly of the type IV secretion apparatus."

H J Yeo, S N Savvides, A B Herr, E Lanka, G Waksman (2000). Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system. Mol Cell, 6:1461-72 [Medline info for 11163218]
Savvas N Savvides, Hye-Jeong Yeo, Moriah R Beck, Franca Blaesing, Rudi Lurz, Erich Lanka, Renate Buhrdorf, Wolfgang Fischer, Rainer Haas, Gabriel Waksman (2003). VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion. EMBO J, 22:1969-80 [Medline info for 12727865]

GO terms associated with structures
Molecular functionATP binding
Cellular componentintracellular
Biological processtransport


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
HP0525 1g6o [ B ] 1nlz [ B ] 324

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_