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

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Kudryashev,  Misha       
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;
Buchmann Institute for Molecular Life Sciences, Frankfurt am Main, Germany;

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Citation

Wang, J., Brackmann, M., Castaño-Díez, D., Kudryashev, M., Goldie, K. N., Maier, T., et al. (2017). Cryo-EM structure of the extended type VI secretion system sheath–tube complex. Nature Microbiology, 2, 1507-1512. doi:doi:10.1038/s41564-017-0020-7.


Cite as: https://hdl.handle.net/21.11116/0000-0001-27E5-1
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.