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Title: Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli
Authors: Tran, An X.
Dong, Changjiang
Whitfield, Chris
Keywords: Bacteria
Cell structure
Crystal structure
Endotoxin
Lipopolysaccharide (LPS)
Membrane Biogenesis
Membrane proteins
Membrane trafficking
LPS export
Lpt proteins
QD Chemistry
Issue Date: 22-Oct-2010
Citation: Tran , 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 .
Abstract: LptC 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.
Version: Publisher PDF
Description: This work is supported by a Wellcome Trust Career Development Fellowship to C.D.
Status: Peer reviewed
URI: http://hdl.handle.net/10023/2880
DOI: http://dx.doi.org/10.1074/jbc.M110.144709
ISSN: 0021-9258
Type: Journal article
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.
Appears in Collections:University of St Andrews Research
Chemistry Research
Biomedical Sciences Research Complex (BSRC) Research



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