Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli

An X. Tran, Changjiang Dong, Chris Whitfield

Research output: Contribution to journalArticlepeer-review

93 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)33529-33539
Number of pages11
JournalJournal of Biological Chemistry
Volume285
Issue number43
Early online date18 Aug 2010
DOIs
Publication statusPublished - 22 Oct 2010

Keywords

  • Bacteria
  • Cell structure
  • Crystal structure
  • Endotoxin
  • Lipopolysaccharide (LPS)
  • Membrane Biogenesis
  • Membrane proteins
  • Membrane trafficking
  • LPS export
  • Lpt proteins

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