Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

被引：61

作者：

Estrozi, Leandro F. ^{[2
,3
]}

Boehringer, Daniel ^{[1
]}

Shan, Shu-ou ^{[4
]}

Ban, Nenad ^{[1
]}

Schaffitzel, Christiane ^{[2
,3
]}

机构：

[1] ETH Zurich Swiss Fed Inst Technol, Inst Mol Biol & Biophys, Zurich, Switzerland

[2] European Mol Biol Lab, F-38042 Grenoble, France

[3] Unit Virus Host Cell Interact, Unite Mixte Int 3265, Grenoble, France

[4] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 01期

基金：

瑞士国家科学基金会;

关键词：

SIGNAL-RECOGNITION PARTICLE; CRYSTAL-STRUCTURE; RNA; MEMBRANE; BINDING; SEQUENCE; DOMAIN; CORE; FTSY;

D O I：

10.1038/nsmb.1952

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 report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.

引用

页码：88 / 90

页数：3

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