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dc.contributor.author
Rapisarda, Chiara
dc.contributor.author
Cherrak, Yassine
dc.contributor.author
Kooger, Romain
dc.contributor.author
Schmidt, Victoria
dc.contributor.author
Pellarin, Riccardo
dc.contributor.author
Logger, Laureen
dc.contributor.author
Cascales, Eric
dc.contributor.author
Pilhofer, Martin
dc.contributor.author
Durand, Eric
dc.contributor.author
Fronzes, Rémi
dc.date.accessioned
2022-01-10T12:15:16Z
dc.date.available
2019-06-01T02:30:30Z
dc.date.available
2019-06-03T09:58:19Z
dc.date.available
2022-01-10T12:15:16Z
dc.date.issued
2019-05-15
dc.identifier.issn
0261-4189
dc.identifier.issn
1460-2075
dc.identifier.other
10.15252/embj.2018100886
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/344967
dc.identifier.doi
10.3929/ethz-b-000344967
dc.description.abstract
Bacteria have evolved macromolecular machineries that secrete effectors and toxins to survive and thrive in diverse environments. The type VI secretion system (T6SS) is a contractile machine that is related to Myoviridae phages. It is composed of a phage tail‐like structure inserted in the bacterial cell envelope by a membrane complex (MC) comprising the TssJ, TssL and TssM proteins. We previously reported the low‐resolution negative‐stain electron microscopy structure of the enteroaggregative Escherichia coli MC and proposed a rotational 5‐fold symmetry with a TssJ:TssL:TssM stoichiometry of 2:2:2. Here, cryo‐electron tomography analyses of the T6SS MC confirm the 5‐fold symmetry in situ and identify the regions of the structure that insert into the bacterial membranes. A high‐resolution model obtained by single‐particle cryo‐electron microscopy highlights new features: five additional copies of TssJ, yielding a TssJ:TssL:TssM stoichiometry of 3:2:2, an 11‐residue loop in TssM, protruding inside the lumen of the MC and constituting a functionally important periplasmic gate, and hinge regions. Based on these data, we propose an updated model on MC structure and dynamics during T6SS assembly and function.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Wiley
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject
cryo-electron microscopy
en_US
dc.subject
membrane protein complex
en_US
dc.subject
type VI secretion systems
en_US
dc.title
In situ and high-resolution cryo-EM structure of a bacterial type VI secretion system membrane complex
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
dc.date.published
2019-03-15
ethz.journal.title
The EMBO Journal
ethz.journal.volume
38
en_US
ethz.journal.issue
10
en_US
ethz.journal.abbreviated
EMBO J
ethz.pages.start
e100886
en_US
ethz.size
18 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Multiscale model of bacterial cell-cell interactions
en_US
ethz.identifier.scopus
ethz.publication.place
Weinheim
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09463 - Pilhofer, Martin / Pilhofer, Martin
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::09463 - Pilhofer, Martin / Pilhofer, Martin
ethz.grant.agreementno
679209
ethz.grant.fundername
EC
ethz.grant.funderDoi
10.13039/501100000780
ethz.grant.program
H2020
ethz.date.deposited
2019-06-01T02:30:36Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2019-06-03T09:58:46Z
ethz.rosetta.lastUpdated
2022-03-29T17:26:24Z
ethz.rosetta.versionExported
true
ethz.COinS
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