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

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Item Type:	Article
Title:	Cryo-EM structure of the extended type VI secretion system sheath-tube complex
Creators Name:	Wang, J., Brackmann, M., Castaño-Díez, D., Kudryashev, M., Goldie, K.N., Maier, T., Stahlberg, H. and Basler, M.
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. 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.
Keywords:	Bacterial Proteins, Cryoelectron Microscopy, Molecular Models, Spheroplasts, Type VI Secretion Systems, Vibrio cholerae
Source:	Nature Microbiology
ISSN:	2058-5276
Publisher:	Nature Publishing Group
Volume:	2
Number:	11
Page Range:	1507-1512
Date:	November 2017
Official Publication:	https://doi.org/10.1038/s41564-017-0020-7
PubMed:	View item in PubMed

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