Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements

被引：406

作者：

Korostelev, Andrei

Trakhanov, Sergei

Laurberg, Martin

Noller, Harry F. ^{[1
]}

机构：

[1] Univ Calif Santa Cruz, Ctr Mol Biol RNA, Santa Cruz, CA 95064 USA

[2] Univ Calif Santa Cruz, Dept Mol Cell & Dev Biol, Santa Cruz, CA 95064 USA

来源：

CELL | 2006年 / 126卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.cell.2006.08.032

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：

Our understanding of the mechanism of protein synthesis has undergone rapid progress in recent years as a result of low-resolution X-ray and cryo-EM structures of ribosome functional complexes and high-resolution structures of ribosomal subunits and vacant ribosomes. Here, we present the crystal structure of the Thermus thermophilus 70S ribosome containing a model mRNA and two tRNAs at 3.7 angstrom resolution. Many structural details of the interactions between the ribosome, tRNA, and mRNA in the P and E sites and the ways in which tRNA structure is distorted by its interactions with the ribosome are seen. Differences between the conformations of vacant and tRNA-bound 70S ribosomes suggest an induced fit of the ribosome structure in response to tRNA binding, including significant changes in the peptidyl-transferase catalytic site.

引用

收藏

页码：1065 / 1077

页数：13

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