Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome
Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome
复制标题
DOI：
10.1126/science.1164840
复制
发表时间：
2008-11-07
期刊：
影响因子：
56.9
通讯作者：
Ramakrishnan, Venki
中科院分区：
文献类型：
--
作者：
Weixlbaumer, Albert;Jin, Hong;Ramakrishnan, Venki
蛋白质合成的终止是通过释放因子 (RF) 对核糖体 A 位点中的终止密码子的特异性识别而发生的，然后催化来自 P 位点转移 RNA 的新生蛋白质链的水解。在这里，我们以 3.5 埃的分辨率展示了 RF2 与其同源 UGA 终止密码子在 70S 核糖体中复合的晶体结构。该结构让我们深入了解 RF2 如何特异性识别终止密码子；它还提出了一个普遍保守的 GGQ 基序在肽释放催化中的作用模型。
The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor ( RF), which then catalyzes the hydrolysis of the nascent protein chain from the P- site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.