Molecular Architecture of a Eukaryotic Translational Initiation Complex

被引：110

作者：

Fernandez, Israel S. ^{[1
]}

Bai, Xiao-Chen ^{[1
]}

Hussain, Tanweer ^{[1
]}

Kelley, Ann C. ^{[1
]}

Lorsch, Jon R. ^{[2
]}

Ramakrishnan, V. ^{[1
]}

Scheres, Sjors H. W. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Johns Hopkins Univ, Sch Med, Baltimore, MD 21205 USA

来源：

SCIENCE | 2013年 / 342卷 / 6160期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

CRYO-EM STRUCTURE; RIBOSOMAL-SUBUNIT; CRYSTAL-STRUCTURE; TRANSFER-RNA; MECHANISMS;

D O I：

10.1126/science.1240585

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：

The last step in eukaryotic translational initiation involves the joining of the large and small subunits of the ribosome, with initiator transfer RNA (Met-tRNA(i)(Met)) positioned over the start codon of messenger RNA in the P site. This step is catalyzed by initiation factor eIF5B. We used recent advances in cryo-electron microscopy (cryo-EM) to determine a structure of the eIF5B initiation complex to 6.6 angstrom resolution from <3% of the population, comprising just 5143 particles. The structure reveals conformational changes in eIF5B, initiator tRNA, and the ribosome that provide insights into the role of eIF5B in translational initiation. The relatively high resolution obtained from such a small fraction of a heterogeneous sample suggests a general approach for characterizing the structure of other dynamic or transient biological complexes.

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页码：824 / +

页数：7

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