70S核糖体 - tRNA复合物的晶体结构揭示了功能相互作用和重排。

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

作者信息

Korostelev Andrei, Trakhanov Sergei, Laurberg Martin, Noller Harry F

机构信息

Center for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz, CA 95064, USA.

出版信息

Cell. 2006 Sep 22;126(6):1065-77. doi: 10.1016/j.cell.2006.08.032. Epub 2006 Sep 7.

DOI:10.1016/j.cell.2006.08.032

PMID:16962654

Abstract

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 A 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.

摘要

近年来，由于核糖体功能复合物的低分辨率X射线和冷冻电镜结构以及核糖体亚基和空核糖体的高分辨率结构，我们对蛋白质合成机制的理解取得了迅速进展。在此，我们展示了嗜热栖热菌70S核糖体的晶体结构，其包含一个模型mRNA和两个处于3.7埃分辨率的tRNA。我们可以看到核糖体、tRNA和mRNA在P位和E位之间相互作用的许多结构细节，以及tRNA结构因与核糖体相互作用而发生扭曲的方式。空的和结合了tRNA的70S核糖体构象之间的差异表明，核糖体结构会因tRNA结合而发生诱导契合，包括肽基转移酶催化位点的显著变化。