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In situ structural analysis of the Yersinia enterocolitica injectisome

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Item Type:Article
Title:In situ structural analysis of the Yersinia enterocolitica injectisome
Creators Name:Kudryashev, M. and Stenta, M. and Schmelz, S. and Amstutz, M. and Wiesand, U. and Castaño-Díez, D. and Degiacomi, M.T. and Münnich, S. and Bleck, C.K. and Kowal, J. and Diepold, A. and Heinz, D.W. and Dal Peraro, M. and Cornelis, G.R. and Stahlberg, H.
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.
Keywords:Cryoelectron Microscopy, Membrane Proteins, Osmotic Pressure, Protein Conformation, Yersinia enterocolitica
Publisher:eLife Sciences Publications
Page Range:e00792
Date:30 July 2013
Official Publication:https://doi.org/10.7554/eLife.00792
PubMed:View item in PubMed

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