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Cryo-EM structure of the extended type VI secretion system sheath-tube complex

Wang, Jing and Brackmann, Maximilian and Castaño-Díez, Daniel and Kudryashev, Mikhail and Goldie, Kenneth N. and Maier, Timm and Stahlberg, Henning and Basler, Marek. (2017) Cryo-EM structure of the extended type VI secretion system sheath-tube complex. Nature Microbiology.

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Official URL: http://edoc.unibas.ch/56324/

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Abstract

The bacterial type VI secretion system (T6SS) uses contraction of a long sheath to quickly thrust a tube with associated effectors across membranes of eukaryotic and bacterial cells (1-5) . Only limited structural information is available about the inherently unstable precontraction state of the T6SS. Here, we obtain a 3.7 Å resolution structure of a non-contractile sheath-tube complex using cryo-electron microscopy and show that it resembles the extended T6SS inside Vibrio cholerae cells. We build a pseudo-atomic model of the complete sheath-tube assembly, which provides a mechanistic understanding of coupling sheath contraction with pushing and rotating the inner tube for efficient target membrane penetration. Our data further show that sheath contraction exposes a buried recognition domain to specifically trigger the disassembly and recycling of the T6SS sheath by the cognate ATP-dependent unfoldase ClpV.The structure of the extended sheath-tube complex of the type VI secretion system from Vibrio cholerae elucidates the molecular mechanisms by which conformational changes in the sheath enable the inner tube to penetrate target cells.The structure of the extended sheath-tube complex of the type VI secretion system from Vibrio cholerae elucidates the molecular mechanisms by which conformational changes in the sheath enable the inner tube to penetrate target cells.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Infection Biology (Basler)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning and Maier, Timm and Basler, Marek and ,
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
e-ISSN:2058-5276
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:17 Oct 2017 13:49
Deposited On:13 Oct 2017 08:00

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