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| Item Type: | Article |
|---|---|
| Title: | Cryo-EM structure of the extended type VI secretion system sheath-tube complex |
| Creators: |
Wang, J.  ORCID: https://orcid.org/0000-0001-8218-1981, Brackmann, M. ORCID: https://orcid.org/0000-0003-0079-1693, Castaño-Díez, D., Kudryashev, M. ORCID: https://orcid.org/0000-0003-3550-6274, Goldie, K.N., Maier, T. ORCID: https://orcid.org/0000-0002-7459-1363, Stahlberg, H. ORCID: https://orcid.org/0000-0002-1185-4592 and Basler, M. ORCID: https://orcid.org/0000-0001-5414-2088
|
| 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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