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  VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion

Savvides, S. N., Yeo, H.-J., Beck, M. R., Blaesing, F., Lurz, R., Lanka, E., et al. (2003). VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion. EMBO Journal, 22(9), 1969-1980.

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Genre: Journal Article
Alternative Title : Embo J.

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 Creators:
Savvides, Savvas N., Author
Yeo, Hye-Jeong, Author
Beck, Moriah R., Author
Blaesing, Franca1, Author           
Lurz, Rudi2, Author
Lanka, Erich2, Author
Buhrdorf, Renate, Author
Fischer, Wolfgang, Author
Haas, Rainer, Author
Waksman, Gabriel, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              

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Free keywords: bacterial pathogenesis; crystal structure; Helicobacter pylori; HP0525; VirB11 ATPases
 Abstract: The coupling of ATP binding/hydrolysis to macromolecular secretion systems is crucial to the pathogenicity of Gram-negative bacteria. We reported previously the structure of the ADP-bound form of the hexameric traffic VirB11 ATPase of the Helicobacter pylori type IV secretion system (named HP0525), and proposed that it functions as a gating molecule at the inner membrane, cycling through closed and open forms regulated by ATP binding/hydrolysis. Here, we combine crystal structures with analytical ultracentrifugation experiments to show that VirB11 ATPases indeed function as dynamic hexameric assemblies. 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. Bio chemical characterization of mutant forms of HP0525 coupled with electron microscopy and in vivo assays support such hypothesis, and establish the relevance of VirB11s ATPases as drug targets against pathogenic bacteria.

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Language(s): eng - English
 Dates: 2003-05-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 173742
ISI: 000182630900005
 Degree: -

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Title: EMBO Journal
  Alternative Title : Embo J.
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 22 (9) Sequence Number: - Start / End Page: 1969 - 1980 Identifier: ISSN: 0261-4189