Solution NMR Studies of Membrane-Protein-Chaperone Complexes

被引:13
作者
Burmann, Bjoern M. [1 ]
Hiller, Sebastian [1 ]
机构
[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
基金
瑞士国家科学基金会;
关键词
beta-Barrel membrane proteins; Membrane biogenesis; Molecular chaperones; NMR spectroscopy; Protein complexes; Protein folding; TRIGGER FACTOR; MOLECULAR CHAPERONE; RESIDUAL STRUCTURE; CRYSTAL-STRUCTURE; DENATURED STATE; SURA; SKP; SUBSTRATE; PEPTIDES; BINDING;
D O I
10.2533/chimia.2012.759
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:759 / 763
页数:5
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