The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor

被引：115

作者：

Ataide, Sandro F. ^{[3
]}

Schmitz, Nikolaus ^{[3
]}

Shen, Kuang ^{[4
]}

Ke, Ailong ^{[5
]}

Shan, Shu-ou ^{[4
]}

Doudna, Jennifer A. ^{[1
,2
]}

Ban, Nenad ^{[3
]}

机构：

[1] Univ Calif Berkeley, Dept Chem, Howard Hughes Med Inst, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA

[3] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

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

[5] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA

来源：

SCIENCE | 2011年 / 331卷 / 6019期

基金：

瑞士国家科学基金会;

关键词：

SRP GTPASES FFH; ESCHERICHIA-COLI; CONFORMATIONAL-CHANGES; TRANSLATING RIBOSOME; NUCLEOTIDE SPECIFICITY; 4.5S RNA; FTSY; BINDING; DOMAIN; CORE;

D O I：

10.1126/science.1196473

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP: SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP: SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP: SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon.

引用

页码：881 / 886

页数：6

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