Repositioning of Transmembrane α-Helices during Membrane Protein Folding

JOURNAL OF MOLECULAR BIOLOGY

卷:397

Article

Elofsson, Arne¹ 

[1] Stockholm Univ, Ctr Biomembrane Res, SE-10691 Stockholm, Sweden

关键词: membrane protein;    Glt(Ph);    protein folding;    membrane insertion;   

DOI  :  10.1016/j.jmb.2010.01.042

来源: Elsevier

【 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

【 授权许可】

Free