In situ and high-resolution Cryo-EM structure of the Type VI secretion membrane complex
dc.rights.license | open | en_US |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | RAPISARDA, Chiara | |
hal.structure.identifier | Laboratoire d'ingénierie des systèmes macromoléculaires [LISM] | |
dc.contributor.author | CHERRAK, Yassine | |
hal.structure.identifier | Institute of Biochemistry [ETH Zürich] | |
dc.contributor.author | KOOGER, Romain | |
dc.contributor.author | SCHMIDT, Victoria | |
dc.contributor.author | PELLARIN, Riccardo | |
hal.structure.identifier | Laboratoire d'ingénierie des systèmes macromoléculaires [LISM] | |
dc.contributor.author | LOGGER, Laureen | |
dc.contributor.author | CASCALES, Eric | |
hal.structure.identifier | Institute of Biochemistry [ETH Zürich] | |
dc.contributor.author | PILHOFER, Martin | |
dc.contributor.author | DURAND, Eric | |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | FRONZES, Remi | |
dc.date.accessioned | 2023-11-20T15:05:17Z | |
dc.date.available | 2023-11-20T15:05:17Z | |
dc.date.issued | 2019-05-15 | |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/184854 | |
dc.description.abstractEn | 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 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 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 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. | |
dc.language.iso | EN | en_US |
dc.rights | Attribution-NonCommercial-ShareAlike 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/3.0/us/ | * |
dc.subject.en | Bacterial Secretion Systems | |
dc.subject.en | Cell Membrane | |
dc.subject.en | Cryoelectron Microscopy | |
dc.subject.en | Escherichia coli | |
dc.subject.en | Escherichia coli Proteins | |
dc.subject.en | Membrane Proteins | |
dc.subject.en | Models | |
dc.subject.en | Molecular | |
dc.subject.en | Protein Binding | |
dc.subject.en | Protein Structure | |
dc.subject.en | Quaternary | |
dc.subject.en | Type VI Secretion Systems | |
dc.title.en | In situ and high-resolution Cryo-EM structure of the Type VI secretion membrane complex | |
dc.title.alternative | EMBO J | en_US |
dc.type | Article de revue | en_US |
dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie | en_US |
dc.identifier.pubmed | 30877094 | en_US |
bordeaux.journal | EMBO Journal | en_US |
bordeaux.volume | 38 | en_US |
bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
bordeaux.issue | 10 | en_US |
bordeaux.institution | CNRS | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
bordeaux.import.source | pubmed | |
hal.popular | non | en_US |
hal.audience | Internationale | en_US |
hal.export | false | |
workflow.import.source | pubmed | |
dc.rights.cc | Pas de Licence CC | en_US |
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