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dc.contributor.authorBernal, Ivonne
dc.contributor.authorBörnicke, Jonathan
dc.contributor.authorHeidemann, Johannes
dc.contributor.authorSvergun, Dmitri
dc.contributor.authorHorstmann, Julia A
dc.contributor.authorErhardt, Marc
dc.contributor.authorTuukkanen, Anne
dc.contributor.authorUetrecht, Charlotte
dc.contributor.authorKolbe, Michael
dc.date.accessioned2019-08-26T11:18:32Z
dc.date.available2019-08-26T11:18:32Z
dc.date.issued2019-07-06
dc.identifier.citationJ Mol Biol. 2019 Jul 6. pii: S0022-2836(19)30425-5. doi: 10.1016/j.jmb.2019.07.004.en_US
dc.identifier.issn1089-8638
dc.identifier.pmid31288030
dc.identifier.doi10.1016/j.jmb.2019.07.004
dc.identifier.urihttp://hdl.handle.net/10033/621919
dc.description.abstractMany medically relevant Gram-negative bacteria use the type III secretion system (T3SS) to translocate effector proteins into the host for their invasion and intracellular survival. A multi-protein complex located at the cytosolic interface of the T3SS is proposed to act as a sorting platform by selecting and targeting substrates for secretion through the system. However, the precise stoichiometry and 3D organization of the sorting platform components are unknown. Here we reconstitute soluble complexes of the Salmonella Typhimurium sorting platform proteins including the ATPase InvC, the regulator OrgB, the protein SpaO and a recently identified subunit SpaOC, which we show to be essential for the solubility of SpaO. We establish domain-domain interactions, determine for the first time the stoichiometry of each subunit within the complexes by native mass spectrometry and gain insight into their organization using small-angle X-ray scattering. Importantly, we find that in solution the assembly of SpaO/SpaOC/OrgB/InvC adopts an extended L-shaped conformation resembling the sorting platform pods seen in in situ cryo-electron tomography, proposing that this complex is the core building block that can be conceivably assembled into higher oligomers to form the T3SS sorting platform. The determined molecular arrangements of the soluble complexes of the sorting platform provide important insights into its architecture and assembly.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/311374en_US
dc.rightsembargoedAccessen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectHost–pathogen interactionen_US
dc.subjectSalmonella entericaen_US
dc.subjectnative mass spectrometryen_US
dc.subjectprotein complexen_US
dc.subjectsmall-angle X‐ray scattering (SAXS)en_US
dc.titleMolecular Organization of Soluble Type III Secretion System Sorting Platform Complexes.en_US
dc.typeArticleen_US
dc.contributor.departmentCSSB, Centre for Structural Systembiologie, Notkestr.85, 22607 Hamburg. Germany.en_US
dc.identifier.journalJournal of Molecular Biologyen_US
dc.source.journaltitleJournal of molecular biology


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