Structure and structural variations of the Escherichia coli 30 S ribosomal subunit as revealed by three-dimensional cryo-electron microscopy
Structure and structural variations of the Escherichia coli 30 S ribosomal subunit as revealed by three-dimensional cryo-electron microscopy
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DOI：
10.1006/jmbi.1999.2538
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发表时间：
1999-03-12
影响因子：
5.6
通讯作者：
Frank, J
中科院分区：
文献类型：
--
作者：
Gabashvili, IS;Agrawal, RK;Frank, J
以 23 埃分辨率获得了大肠杆菌核糖体 30 S 亚基的三维重建。由于分辨率的提高，与早期研究中获得的结构细节相比，可以看到更多的结构细节。因此，新结构更适合与70S核糖体的30S亚基部分进行比较，70S核糖体的结构已经以更好的分辨率已知。此外，我们观察到 30 S 亚基的三个主要结构域（即头部、平台和主体）相对且在某种程度上独立的运动，这导致重建体积的部分模糊。将数据集细分为构象定义的子集的尝试揭示了构象异构体的存在，其中这些域彼此具有不同的方向。这一结果表明 30 S 亚基存在动态特性，这可能是促进其在蛋白质生物合成过程中与 mRNA、tRNA 和其他配体相互作用所必需的。 (C) 1999 年学术出版社。
A three-dimensional reconstruction of the 30 S subunit of the Escherichia coli ribosome was obtained at 23 Angstrom resolution. Because of the improved resolution, many more structural details are seen as compared to those obtained in earlier studies. Thus, the new structure is more suitable for comparison with the 30 S subunit part of the 70 S ribosome, whose structure is already known at a better resolution. In addition, we observe relative and, to some extent, independent movements of three main structural domains of the 30 S subunit, namely head, platform and the main body, which lead to partial blurring of the reconstructed volume. An attempt to subdivide the data set into conformationally defined subsets reveals the existence of conformers in which these domains have different orientations with respect to one another. This result suggests the existence of dynamic properties of the 30 S subunit that might be required for facilitating its interactions with mRNA, tRNA and other ligands during protein biosynthesis. (C) 1999 Academic Press.