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dc.contributor.authorKaplan, Elise
dc.contributor.authorGreene, Nicholas
dc.contributor.authorCrow, Allister
dc.contributor.authorKoronakis, Vassilis
dc.date.accessioned2018-10-31T06:51:22Z
dc.date.available2018-10-31T06:51:22Z
dc.date.issued2018-07-31
dc.identifier.issn0027-8424
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284440
dc.description.abstractIn Gram-negative bacteria, outer-membrane lipoproteins are essential for maintaining cellular integrity, transporting nutrients, establishing infections, and promoting the formation of biofilms. The LolCDE ABC transporter, LolA chaperone, and LolB outer-membrane receptor form an essential system for transporting newly matured lipoproteins from the outer leaflet of the cytoplasmic membrane to the innermost leaflet of the outer membrane. Here, we present a crystal structure of LolA in complex with the periplasmic domain of LolC. The structure reveals how a solvent-exposed β-hairpin loop (termed the "Hook") and trio of surface residues (the "Pad") of LolC are essential for recruiting LolA from the periplasm and priming it to receive lipoproteins. Experiments with purified LolCDE complex demonstrate that association with LolA is independent of nucleotide binding and hydrolysis, and homology models based on the MacB ABC transporter predict that LolA recruitment takes place at a periplasmic site located at least 50 Å from the inner membrane. Implications for the mechanism of lipoprotein extraction and transfer are discussed. The LolA-LolC structure provides atomic details on a key protein interaction within the Lol pathway and constitutes a vital step toward the complete molecular understanding of this important system.
dc.description.sponsorshipThis work was supported by grants from the UK Medical Research Council (MR/N000994/1) and the Wellcome Trust (101828/Z/13/Z).
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherProceedings of the National Academy of Sciences
dc.subjectPeriplasm
dc.subjectEscherichia coli Proteins
dc.subjectPeriplasmic Binding Proteins
dc.subjectATP-Binding Cassette Transporters
dc.subjectAdenosine Triphosphate
dc.subjectProtein Interaction Mapping
dc.subjectProtein Transport
dc.subjectHydrolysis
dc.subjectModels, Molecular
dc.titleInsights into bacterial lipoprotein trafficking from a structure of LolA bound to the LolC periplasmic domain.
dc.typeArticle
prism.endingPageE7397
prism.issueIdentifier31
prism.publicationDate2018
prism.publicationNameProc Natl Acad Sci U S A
prism.startingPageE7389
prism.volume115
dc.identifier.doi10.17863/CAM.31812
dcterms.dateAccepted2018-06-25
rioxxterms.versionofrecord10.1073/pnas.1806822115
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2018-07-16
dc.contributor.orcidKaplan, Elise [0000-0003-4985-1482]
dc.contributor.orcidGreene, Nicholas [0000-0002-3631-0380]
dc.contributor.orcidCrow, Allister [0000-0001-6856-5962]
dc.contributor.orcidKoronakis, Vassilis [0000-0002-1353-1092]
dc.identifier.eissn1091-6490
rioxxterms.typeJournal Article/Review
pubs.funder-project-idMedical Research Council (MR/N000994/1)
pubs.funder-project-idWellcome Trust (101828/Z/13/Z)
cam.issuedOnline2018-07-16
rioxxterms.freetoread.startdate2019-01-16


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