Accurate protein synthesis (translation) relies on translation factors that rectify ribosome fluctuations into a unidirectional process. Understanding this process requires structural characterization of the ribosome and translation-factor dynamics. In the 2000s, crystallographic studies determined high-resolution structures of ribosomes stalled with translation factors, providing a starting point for visualizing translation. Recent progress in single-particle cryogenic electron microscopy (cryo-EM) has enabled near-atomic resolution of numerous structures sampled in heterogeneous complexes (ensembles). Ensemble and time-resolved cryo-EM have now revealed unprecedented views of ribosome transitions in the three principal stages of translation: initiation, elongation, and termination. This review focuses on how translation factors help achieve high accuracy and efficiency of translation by monitoring distinct ribosome conformations and by differentially shifting the equilibria of ribosome rearrangements for cognate and near-cognate substrates.

中文翻译：

---

翻译的结构动力学

准确的蛋白质合成（翻译）依赖于将核糖体波动纠正为单向过程的翻译因子。了解这一过程需要核糖体和翻译因子动力学的结构表征。 2000 年代，晶体学研究确定了因翻译因子而停滞的核糖体的高分辨率结构，为可视化翻译提供了起点。单粒子低温电子显微镜 (cryo-EM) 的最新进展使得对异质复合物（系综）中采样的众多结构实现了近原子分辨率。整体和时间分辨冷冻电镜现在揭示了翻译的三个主要阶段中核糖体转变的前所未有的观点：起始、延伸和终止。本综述重点关注翻译因素如何通过监测不同的核糖体构象并通过差异性地改变同源和近同源底物的核糖体重排平衡来帮助实现高精度和高效率的翻译。