Structural analysis of a prototypical ATPase from the type III secretion system-Reference-Cited by-同舟云学术

Structural analysis of a prototypical ATPase from the type III secretion system

Published:2007-01-21 Issue:2 Volume:14 Page:131-137
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Zarivach Raz,Vuckovic Marija,Deng Wanyin,Finlay B Brett,Strynadka Natalie C J

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb1196.pdf

Reference41 articles.

1. Hueck, C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62, 379–433 (1998).

2. Gophna, U., Ron, E.Z. & Graur, D. Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events. Gene 312, 151–163 (2003).

3. Bennett, J.C. & Hughes, C. From flagellum assembly to virulence: the extended family of type III export chaperones. Trends Microbiol. 8, 202–204 (2000).

4. Luo, Y. et al. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nat. Struct. Biol. 8, 1031–1036 (2001).

5. Thomas, N.A. et al. CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli. Mol. Microbiol. 57, 1762–1779 (2005).

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