The structure of Get4 reveals an α-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis

被引：20

作者：

Bozkurt, Gunes ^{[1
]}

Wild, Klemens ^{[1
]}

Amlacher, Stefan ^{[1
]}

Hurt, Ed ^{[1
]}

Dobberstein, Bernhard ^{[2
]}

Sinning, Irmgard ^{[1
]}

机构：

[1] Univ Heidelberg, Biochem Ctr, BZH, D-69120 Heidelberg, Germany

[2] Univ Heidelberg, Zentrum Mol Biol, ZMBH, DKFZ,ZMBH Allianz, D-69120 Heidelberg, Germany

来源：

FEBS LETTERS | 2010年 / 584卷 / 08期

关键词：

Get pathway; Posttranslational targeting; Tail-anchored membrane protein insertion; TPR-like fold; MEMBRANE INSERTION; RECOGNITION; COMPLEX; IDENTIFICATION; ARCHITECTURE; LANDSCAPE; BINDING; MODEL; ER;

D O I：

10.1016/j.febslet.2010.02.070

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：

Tail-anchored proteins play important roles in protein translocation, membrane fusion and apoptosis. They are targeted to the endoplasmic reticulum membrane via the guided-entry of tail-anchored proteins ( Get) pathway. We present the 2 angstrom crystal structure of Get4 which participates in early steps of the Get pathway. The structure shows an alpha-solenoid fold with particular deviations from the regular pairwise arrangement of alpha-helices. A conserved hydrophobic groove accommodates the flexible C-terminal region in trans. The structural organization of the Get4 helical hairpin motifs provides a scaffold for protein-protein interactions in the Get pathway. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1509 / 1514

页数：6

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