Repositioning of Transmembrane α-Helices during Membrane Protein Folding

被引：52
作者：
Kauko, Anni
Hedin, Linnea E.
Thebaud, Estelle
Cristobal, Susana
Elofsson, Arne [1 ]
von Heijne, Gunnar
机构：
[1] Stockholm Univ, Ctr Biomembrane Res, SE-10691 Stockholm, Sweden
来源：
JOURNAL OF MOLECULAR BIOLOGY | 2010年 / 397卷 / 01期
基金：
芬兰科学院; 欧洲研究理事会; 瑞典研究理事会;
关键词：
membrane protein; Glt(Ph); protein folding; membrane insertion; ESCHERICHIA-COLI; MOLECULAR CODE; K+ CHANNEL; TOPOLOGY; PREDICTION; RECOGNITION; TRANSLOCATION; MITOCHONDRIA; INTEGRATION; INSERTION;
D O I：
10.1016/j.jmb.2010.01.042
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：
We have determined the optimal placement of individual transmembrane helices in the Pyrococcus horikoshu Glt(Ph) glutamate transporter homolog in the membrane. The results are in close agreement with theoretical predictions based on hydrophobicity, but do not, in general, match the known three-dimensional structure, suggesting that transmembrane helices can be repositioned relative to the membrane during folding and oligomenzation. Theoretical analysis of a database of membrane protein structures provides additional support for this idea. These observations raise new challenges for the structure prediction of membrane proteins and suggest that the classical two-stage model often used to describe membrane protein folding needs to be modified. (C) 2010 Elsevier Ltd All rights reserved
引用
收藏
页码：190 / 201
页数：12
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