The biosynthesis of the bacterial outer membrane depends on molecular chaperones that protect hydrophobic membrane proteins against aggregation while transporting them across the periplasm. In our ongoing research, we use high-resolution NMR spectroscopy in aqueous solution as the main
technique to characterize the structures and biological functions of these membrane-protein–chaperone complexes. Here, we describe NMR studies addressing three functional aspects of periplasmic membrane-protein–chaperone complexes. Firstly, the Escherichia coli outer membrane
protein OmpX binds to each of the two chaperones, Skp and SurA, in structurally at least partially similar states despite fundamental differences between the three-dimensional structures of the chaperones. Secondly, we show that the Skp-bound state of OmpX is equivalent to a chemically denatured
state in terms of its refolding competence into detergent micelles in vitro. Thirdly, we use amino acid mutation analysis to show that the interaction of OmpX to Skp is not dominated by the two most hydrophobic segments of OmpX.
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β-BARREL MEMBRANE PROTEINS
Document Type: Research Article
University of Basel Biozentrum Klingelbergstr. 70 CH-4056 Basel, Switzerland
University of Basel Biozentrum Klingelbergstr. 70 CH-4056 Basel, Switzerland. [email protected]
Publication date: 01 October 2012
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International Journal for Chemistry and Official Membership Journal of the Swiss Chemical Society (SCS) and its Divisions
CHIMIA, a scientific journal for chemistry in the broadest sense, is published 10 times a year and covers the interests of a wide and diverse readership. Contributions from all fields of chemistry and related areas are considered for publication in the form of Review Articles and Notes. A characteristic feature of CHIMIA are the thematic issues, each devoted to an area of great current significance.
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