Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes

被引:133
作者
Knowles, Timothy J. [1 ]
Jeeves, Mark [1 ]
Bobat, Saeeda [2 ]
Dancea, Felician [1 ]
McClelland, Darren [1 ]
Palmer, Tracy [3 ]
Overduin, Michael [1 ]
Henderson, Ian R. [2 ]
机构
[1] Univ Birmingham, Sch Med, Canc Res UK Inst Canc Studies, Birmingham B15 2TT, W Midlands, England
[2] Univ Birmingham, Bacterial Pathogenesis & Genom Unit, Div Immun & Infect, Birmingham B15 2TT, W Midlands, England
[3] Univ Dundee, Coll Life Sci, Dundee DD1 5EH, Scotland
基金
英国医学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
D O I
10.1111/j.1365-2958.2008.06225.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Membranes of Gram-negative bacteria, mitochondria and chloroplasts receive and fold beta-barrel transmembrane proteins through the action of polypeptide transport-associated (POTRA) domains. In Escherichia coli, folding substrates are inserted into the outer membrane by the essential protein YaeT, a prototypic Omp85 protein. Here, the articulation between tandem POTRA domains in solution is defined by nuclear magnetic resonance (NMR) spectroscopy, indicating an unprecedented juxtaposition. The novel solution orientations of all five POTRA domains are revealed by small-angle X-ray scattering of the entire 46 kDa periplasmic region. NMR titration studies show that strands from YaeT's canonical folding substrate, PhoE, bind non-specifically along alternating sides of its mixed beta sheets, thus providing an ideal platform for helping to fold nascent outer-membrane proteins. Together, this provides the first structural model of how multiple POTRA domains recruit substrates from the periplasmic solution into the outer membrane.
引用
收藏
页码:1216 / 1227
页数:12
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