Journal
NATURE MICROBIOLOGY
Volume 2, Issue 11, Pages 1507-1512Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41564-017-0020-7
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Funding
- Swiss National Science Foundation (SNSF) [31003A_159525]
- University of Basel
- SNSF NCCR TransCure
- Swiss National Science Foundation (SNF) [31003A_159525] Funding Source: Swiss National Science Foundation (SNF)
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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 angstrom 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.
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