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  In situ structural analysis of the Yersinia enterocolitica injectisome

Kudryashev, M., Stenta, M., Schmelz, S., Amstutz, M., Wiesand, U., Castaño-Díez, D., et al. (2013). In situ structural analysis of the Yersinia enterocolitica injectisome. eLife, 2: e00792. doi:10.7554/eLife.00792.

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 Creators:
Kudryashev, Misha1, Author              
Stenta, Marco2, Author
Schmelz, Stefan3, Author
Amstutz, Marlise4, Author
Wiesand, Ulrich3, 4, Author
Castaño-Díez, Daniel1, Author
Degiacomi, Matteo T2, Author
Münich, Stefan3, Author
Bleck, Christopher K.E.1, Author
Kowal, Julia1, Author
Diepold, Andreas4, Author
Heinz, Dirk W.3, Author
Dal Peraro, Matteo2, 5, Author
Cornelis, Guy R.4, Author
Stahlberg, Henning1, Author
Affiliations:
1Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, 4058 Basel, Switzerland, ou_persistent22              
2Institute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland, ou_persistent22              
3Division of Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany, ou_persistent22              
4Focal Area Infection Biology, Biozentrum, University Basel, Basel, Switzerland, ou_persistent22              
5Swiss Institute of Bioinformatics (SIB), Lausanne, Switzerland, ou_persistent22              

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 Abstract: Injectisomes are multi-protein transmembrane machines allowing pathogenic bacteria to inject effector proteins into eukaryotic host cells, a process called type III secretion. Here we present the first three-dimensional structure of Yersinia enterocolitica and Shigella flexneri injectisomes in situ and the first structural analysis of the Yersinia injectisome. Unexpectedly, basal bodies of injectisomes inside the bacterial cells showed length variations of 20%. The in situ structures of the Y. enterocolitica and S. flexneri injectisomes had similar dimensions and were significantly longer than the isolated structures of related injectisomes. The crystal structure of the inner membrane injectisome component YscD appeared elongated compared to a homologous protein, and molecular dynamics simulations documented its elongation elasticity. The ring-shaped secretin YscC at the outer membrane was stretched by 30–40% in situ, compared to its isolated liposome-embedded conformation. We suggest that elasticity is critical for some two-membrane spanning protein complexes to cope with variations in the intermembrane distance

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Language(s): eng - English
 Dates: 2013-03-292013-06-272013-07-30
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.00792
PMID: 23908767
PMC: PMC3728920
 Degree: -

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 2 Sequence Number: e00792 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X