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Updated: Jun 22, 2026

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
Published on: November 29, 2014
Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of
Shin-ichiro Narita1, Hajime Tokuda
1Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo, Japan.
Abstract:
Seven Lpt proteins (A through G) are thought to be involved in lipopolysaccharide transport from the inner to outer membrane of Escherichia coli. LptB belongs to the ATP-binding cassette transporter superfamily. Although the lptB gene lacks neighboring genes encoding membrane subunits, bioinformatic analyses recently indicated that two distantly located consecutive genes, lptF and lptG, could encode membrane subunits. To examine this possibility, LptB was expressed with LptF and LptG. We report here that both LptF and LptG formed a complex with LptB. Furthermore, an inner membrane protein, LptC, which had been implicated in lipopolysaccharide transport, was also included in this complex.
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