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dc.contributor.authorBiou, Valérie
dc.contributor.authorAdaixo, Ricardo Jorge Diogo
dc.contributor.authorChami, Mohamed
dc.contributor.authorCoureux, Pierre-Damien
dc.contributor.authorLaurent, Benoist
dc.contributor.authorEnguéné, Véronique Yvette Ntsogo
dc.contributor.authorde Amorim, Gisele Cardoso
dc.contributor.authorIzadi-Pruneyre, Nadia
dc.contributor.authorMalosse, Christian
dc.contributor.authorChamot-Rooke, Julia
dc.contributor.authorStahlberg, Henning
dc.contributor.authorDelepelaire, Philippe
dc.date.accessioned2022-05-16T01:02:34Z
dc.date.available2022-05-16T01:02:34Z
dc.date.issued2022-04-13
dc.identifier.issn2399-3642
dc.identifier.other35418619
dc.identifier.otherPMC9008036
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337180
dc.description.abstractExbB and ExbD are cytoplasmic membrane proteins that associate with TonB to convey the energy of the proton-motive force to outer membrane receptors in Gram-negative bacteria for iron uptake. The opportunistic pathogen Serratia marcescens (Sm) possesses both TonB and a heme-specific TonB paralog, HasB. ExbB<sub>Sm</sub> has a long periplasmic extension absent in other bacteria such as E. coli (Ec). Long ExbB's are found in several genera of Alphaproteobacteria, most often in correlation with a hasB gene. We investigated specificity determinants of ExbB<sub>Sm</sub> and HasB. We determined the cryo-EM structures of ExbB<sub>Sm</sub> and of the ExbB-ExbD<sub>Sm</sub> complex from S. marcescens. ExbB<sub>Sm</sub> alone is a stable pentamer, and its complex includes two ExbD monomers. We showed that ExbB<sub>Sm</sub> extension interacts with HasB and is involved in heme acquisition and we identified key residues in the membrane domain of ExbB<sub>Sm</sub> and ExbB<sub>Ec</sub>, essential for function and likely involved in the interaction with TonB/HasB. Our results shed light on the class of inner membrane energy machinery formed by ExbB, ExbD and HasB.
dc.languageeng
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourcenlmid: 101719179
dc.sourceessn: 2399-3642
dc.subjectEscherichia coli
dc.subjectSerratia marcescens
dc.subjectHeme
dc.subjectEscherichia coli Proteins
dc.subjectProtein Binding
dc.titleStructural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog.
dc.typeArticle
dc.date.updated2022-05-16T01:02:34Z
prism.issueIdentifier1
prism.publicationNameCommunications biology
prism.volume5
dc.identifier.doi10.17863/CAM.84599
rioxxterms.versionofrecord10.1038/s42003-022-03306-y
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidBiou, Valérie [0000-0003-1600-6717]
dc.contributor.orcidCoureux, Pierre-Damien [0000-0002-1328-7229]
dc.contributor.orcidEnguéné, Véronique Yvette Ntsogo [0000-0003-0096-3192]
dc.contributor.orcidde Amorim, Gisele Cardoso [0000-0003-4348-9515]
dc.contributor.orcidIzadi-Pruneyre, Nadia [0000-0002-6864-2961]
dc.contributor.orcidChamot-Rooke, Julia [0000-0002-9427-543X]
dc.contributor.orcidDelepelaire, Philippe [0000-0002-5190-7118]


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International