Structural basis of signal-sequence recognition by the signal recognition particle

被引:67
作者
Hainzl, Tobias [1 ]
Huang, Shenghua [1 ]
Merilainen, Gitte [1 ]
Brannstrom, Kristoffer [2 ]
Sauer-Eriksson, A. Elisabeth [1 ]
机构
[1] Umea Univ, Dept Chem, Umea, Sweden
[2] Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden
基金
瑞典研究理事会;
关键词
SRP RNA; CRYSTAL-STRUCTURE; GTPASE DOMAIN; 4.5S RNA; RECEPTOR; COMPLEX; PROTEINS; RIBOSOME; BINDING; CORE;
D O I
10.1038/nsmb.1994
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
The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-angstrom structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180 degrees flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.
引用
收藏
页码:389 / 391
页数:3
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