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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorRAPISARDA, Chiara
hal.structure.identifierLaboratoire d'ingénierie des systèmes macromoléculaires [LISM]
dc.contributor.authorCHERRAK, Yassine
hal.structure.identifierInstitute of Biochemistry [ETH Zürich]
dc.contributor.authorKOOGER, Romain
dc.contributor.authorSCHMIDT, Victoria
dc.contributor.authorPELLARIN, Riccardo
hal.structure.identifierLaboratoire d'ingénierie des systèmes macromoléculaires [LISM]
dc.contributor.authorLOGGER, Laureen
dc.contributor.authorCASCALES, Eric
hal.structure.identifierInstitute of Biochemistry [ETH Zürich]
dc.contributor.authorPILHOFER, Martin
dc.contributor.authorDURAND, Eric
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorFRONZES, Remi
dc.date.accessioned2023-11-20T15:05:17Z
dc.date.available2023-11-20T15:05:17Z
dc.date.issued2019-05-15
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184854
dc.description.abstractEnBacteria 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.isoENen_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subject.enBacterial Secretion Systems
dc.subject.enCell Membrane
dc.subject.enCryoelectron Microscopy
dc.subject.enEscherichia coli
dc.subject.enEscherichia coli Proteins
dc.subject.enMembrane Proteins
dc.subject.enModels
dc.subject.enMolecular
dc.subject.enProtein Binding
dc.subject.enProtein Structure
dc.subject.enQuaternary
dc.subject.enType VI Secretion Systems
dc.title.enIn situ and high-resolution Cryo-EM structure of the Type VI secretion membrane complex
dc.title.alternativeEMBO Jen_US
dc.typeArticle de revueen_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed30877094en_US
bordeaux.journalEMBO Journalen_US
bordeaux.volume38en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue10en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=EMBO%20Journal&rft.date=2019-05-15&rft.volume=38&rft.issue=10&rft.eissn=1460-2075&rft.issn=1460-2075&rft.au=RAPISARDA,%20Chiara&CHERRAK,%20Yassine&KOOGER,%20Romain&SCHMIDT,%20Victoria&PELLARIN,%20Riccardo&rft.genre=article


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