The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells

DC FieldValueLanguage
dc.contributor.authorGalazzo, Laura
dc.contributor.authorMeier, Gianmarco
dc.contributor.authorJanuliene, Dovile
dc.contributor.authorParey, Kristian
dc.contributor.authorDe Vecchis, Dario
dc.contributor.authorStriednig, Bianca
dc.contributor.authorHilbi, Hubert
dc.contributor.authorSchaefer, V, Lars
dc.contributor.authorKuprov, Ilya
dc.contributor.authorMoeller, Arne
dc.contributor.authorBordignon, Enrica
dc.contributor.authorSeeger, Markus A.
dc.date.accessioned2023-02-17T11:36:20Z-
dc.date.available2023-02-17T11:36:20Z-
dc.date.issued2022
dc.identifier.issn2375-2548
dc.identifier.urihttp://osnascholar.ub.uni-osnabrueck.de/handle/unios/65575-
dc.description.abstractMembrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in Escherichia coli cells. Molecular dynamics simulations revealed that extensive lateral portal opening is essential to provide access of its large natural substrate core lipid A to the binding cavity. Our work paves the way to investigate the conformational landscape of membrane proteins in cells.
dc.description.sponsorshipLeverhulme Trust [RPG-2019-048]; MathWorks and used NVIDIA Tesla A100 GPUs through NVIDIA Academic Grants Programme; DFG [CRC944]; Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [EXC 2033-390677874, SCHA 1574/6-1]; European Research Council (ERC) [772190]; SNSF Professorship of the Swiss National Science Foundation [PP00P3_144823]; Swiss National Science Foundation [310030_188817]; Research in the laboratory of I.K. was supported by grants from Leverhulme Trust (RPG-2019-048) and MathWorks and used NVIDIA Tesla A100 GPUs through NVIDIA Academic Grants Programme. Research in the laboratory of A.M. was funded by DFG through CRC944. Research in the laboratory of E.B. and L.V.S. was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy-EXC 2033-390677874-RESOLV and grant SCHA 1574/6-1. Research in the laboratory of M.A.S. was funded by the European Research Council (ERC) (consolidator grant no. 772190), an SNSF Professorship of the Swiss National Science Foundation (PP00P3_144823), and a project grant of the Swiss National Science Foundation (310030_188817).
dc.language.isoen
dc.publisherAMER ASSOC ADVANCEMENT SCIENCE
dc.relation.ispartofSCIENCE ADVANCES
dc.subjectATP-BINDING
dc.subjectBINDING CASSETTE TRANSPORTER
dc.subjectCRYO-EM
dc.subjectCRYSTAL-STRUCTURE
dc.subjectESCHERICHIA-COLI
dc.subjectFLEXIBILITY
dc.subjectMOLECULAR-DYNAMICS
dc.subjectMultidisciplinary Sciences
dc.subjectNANOBODIES
dc.subjectP-GLYCOPROTEIN REVEAL
dc.subjectScience & Technology - Other Topics
dc.subjectSTRUCTURAL BASIS
dc.titleThe ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells
dc.typejournal article
dc.identifier.doi10.1126/sciadv.abn6845
dc.identifier.isiISI:000872371200005
dc.description.volume8
dc.description.issue41
dc.contributor.orcid0000-0002-4842-6479
dc.contributor.orcid0000-0002-8498-3061
dc.contributor.orcid0000-0002-3279-7590
dc.contributor.orcid0000-0003-2450-5161
dc.contributor.orcid0000-0001-8440-1757
dc.contributor.orcid0000-0002-7732-5095
dc.publisher.place1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
dcterms.isPartOf.abbreviationSci. Adv.
dcterms.oaStatusGreen Published
local.import.remainsaffiliations : Ruhr University Bochum; University of Geneva; University of Zurich; University Osnabruck; Ruhr University Bochum; University of Southampton
local.import.remainsweb-of-science-index : Science Citation Index Expanded (SCI-EXPANDED)
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-3279-7590-
crisitem.author.orcid0000-0002-4842-6479-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidJaDo206-
crisitem.author.netidMoAr687-
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