Crystal structure of the ribosome at 5.5 Å resolution
Crystal structure of the ribosome at 5.5 Å resolution
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DOI：
10.1126/science.1060089
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发表时间：
2001-05-04
期刊：
影响因子：
56.9
通讯作者：
Noller, HF
中科院分区：
文献类型：
--
作者：
Yusupov, MM;Yusupova, GZ;Noller, HF
我们在5.5埃分辨率下描述了完整的Thermus thermoophilus 70S核糖体的晶体结构，该核糖体含有结合的信使RNA和转移RNA （tRNAs）。所有的16S、23S和5S核糖体RNA （rRNA）链，A-、P-和e -位点trna，以及大多数核糖体蛋白都可以拟合到电子密度图上。tRNA底物结合的30S小亚基和50S大亚基之间的界面核心以RNA为主，蛋白质主要位于外周，与核糖体功能以rRNA为基础一致。在三个tRNA结合位点中的每一个，核糖体都与tRNA的所有主要元素接触，这为tRNA结构的保存提供了解释。tRNA与亚基间桥紧密并列，在某种程度上表明与tRNA易位相关的20至50埃运动与亚基间运动耦合。
We describe the crystal structure of the complete Thermus thermophilus 70S ribosome containing bound messenger RNA and transfer RNAs (tRNAs) at 5.5 angstrom resolution. All of the 16S, 23S, and 5S ribosomal RNA (rRNA) chains, the A-, P-, and E-site tRNAs, and most of the ribosomal proteins can be fitted to the electron density map. The core of the interface between the 30S small subunit and the 50S large subunit, where the tRNA substrates are bound, is dominated by RNA, with proteins located mainly at the periphery, consistent with ribosomal function being based on rRNA. In each of the three tRNA binding sites, the ribosome contacts all of the major elements of tRNA, providing an explanation for the conservation of tRNA structure. The tRNAs are closely juxtaposed with the intersubunit bridges, in a way that suggests coupling of the 20 to 50 angstrom movements associated with tRNA translocation with intersubunit movement.