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Solution NMR studies of membrane-protein-chaperone complexes

Burmann, Björn M. and Hiller, Sebastian. (2012) Solution NMR studies of membrane-protein-chaperone complexes. Chimia, 66 (10). pp. 759-763.

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Official URL: http://edoc.unibas.ch/dok/A6018479

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Abstract

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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Schweizerische Chemische Gesellschaft
ISSN:0009-4293
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:13 Dec 2017 12:10
Deposited On:01 Feb 2013 08:42

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