Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLptC 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 towards the periplasm. The structure of the periplasmic domain is described at a resolution of 2.2-angstroms 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 anti-parallel 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. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coll.,Tran AX, Dong C, Whitfield C J Biol Chem. 2010 Aug 18. PMID:20720015[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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