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dc.contributor.authorTran, An X.
dc.contributor.authorDong, Changjiang
dc.contributor.authorWhitfield, Chris
dc.date.accessioned2012-07-02T10:01:06Z
dc.date.available2012-07-02T10:01:06Z
dc.date.issued2010-10-22
dc.identifier.citationTran , A X , Dong , C & Whitfield , C 2010 , ' Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli ' , Journal of Biological Chemistry , vol. 285 , no. 43 , pp. 33529-33539 . https://doi.org/10.1074/jbc.M110.144709en
dc.identifier.issn0021-9258
dc.identifier.otherPURE: 23332318
dc.identifier.otherPURE UUID: 66a27a26-6906-479a-8f38-6c02212aaba7
dc.identifier.otherWOS: 000283048200087
dc.identifier.otherScopus: 77958502198
dc.identifier.urihttps://hdl.handle.net/10023/2880
dc.descriptionThis work is supported by a Wellcome Trust Career Development Fellowship to C.D.en
dc.description.abstractLptC is a conserved bitopic inner membrane protein from Escherichia coli involved in the export of lipopolysaccharide from its site of synthesis in the cytoplasmic membrane to the outer membrane. LptC forms a complex with the ATP-binding cassette transporter, LptBFG, which is thought to facilitate the extraction of lipopolysaccharide from the inner membrane and release it into a translocation pathway that includes the putative periplasmic chaperone LptA. Cysteine modification experiments established that the catalytic domain of LptC is oriented toward the periplasm. The structure of the periplasmic domain is described at a resolution of 2.2-angstrom from x-ray crystallographic data. The periplasmic domain of LptC consists of a twisted boat structure with two beta-sheets in apposition to each other. The beta-sheets contain seven and eight antiparallel beta-strands, respectively. This structure bears a high degree of resemblance to the crystal structure of LptA. Like LptA, LptC binds lipopolysaccharide in vitro. In vitro, LptA can displace lipopolysaccharide from LptC (but not vice versa), consistent with their locations and their proposed placement in a unidirectional export pathway.
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofJournal of Biological Chemistryen
dc.rights© 2010 by The American Society for Biochemistry and Molecular Biology, Inc. This is an Author's Choice open access article, available under a Creative Commons Attribution Non-Commercial License.en
dc.subjectBacteriaen
dc.subjectCell structureen
dc.subjectCrystal structureen
dc.subjectEndotoxinen
dc.subjectLipopolysaccharide (LPS)en
dc.subjectMembrane Biogenesisen
dc.subjectMembrane proteinsen
dc.subjectMembrane traffickingen
dc.subjectLPS exporten
dc.subjectLpt proteinsen
dc.subjectQD Chemistryen
dc.subject.lccQDen
dc.titleStructure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia colien
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.identifier.doihttps://doi.org/10.1074/jbc.M110.144709
dc.description.statusPeer revieweden


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