Revisiting the Haloarcula marismortui 50S ribosomal subunit model
Revisiting the Haloarcula marismortui 50S ribosomal subunit model
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DOI：
10.1107/s0907444913004745
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发表时间：
2013-06-01
影响因子：
2.2
通讯作者：
Garber, Maria
中科院分区：
文献类型：
--
作者：
Gabdulkhakov, Azat;Nikonov, Stanislav;Garber, Maria
来自嗜盐古菌Haloarcula marismortui（Hma）的核糖体大亚基的结构是迄今为止已确定的古菌核糖体颗粒的唯一晶体结构。然而，第一个模型的Hma 50 S核糖体亚基包含一些差距：功能上重要的移动的横向突起的结构是不可见的。随后，P（L12）茎基部的一些部分以3.0埃分辨率可视化[Kavran & Steitz（2007），J. Mol. Biol. 371，1047-1059]：r-蛋白P0的RNA结合结构域（L10）、L11的C-末端结构域和23 S rRNA的螺旋43和44。在此，重新审视了Hma 50 S核糖体亚基的2.4埃分辨率电子密度图，并对P0蛋白的大约三分之二、两个P1蛋白分子的N-末端结构域的残基1-58、L11的残基130-156、全长r-蛋白LX、可以看到形成L1茎的23 S rRNA螺旋H76的核苷酸2137-2149和2226-2237、23 S rRNA的核苷酸2339-2343（接触L5蛋白）以及蛋白L5的环29-34和108-128。因此，本文提供了一个补充版本的Hma 50 S核糖体亚基模型。
The structure of the large ribosomal subunit from the halophilic archaeon Haloarcula marismortui (Hma) is the only crystal structure of an archaeal ribosomal particle that has been determined to date. However, the first model of the Hma 50S ribosomal subunit contained some gaps: the structures of functionally important mobile lateral protuberances were not visualized. Subsequently, some parts of the P (L12) stalk base were visualized at 3.0 angstrom resolution [Kavran & Steitz (2007), J. Mol. Biol. 371, 1047-1059]: the RNA-binding domain of r-protein P0 (L10), the C-terminal domain of L11 and helices 43 and 44 of the 23 S rRNA. Here, the 2.4 angstrom resolution electron-density map of the Hma 50S ribosomal subunit was revisited and approximately two-thirds of the P0 protein, residues 1-58 of the N-terminal domains of two P1 protein molecules, residues 130-156 of L11, the full-length r-protein LX, nucleotides 2137-2149 and 2226-2237 of the 23S rRNA helix H76 forming the L1 stalk, nucleotides 2339-2343 of the 23S rRNA (contacting L5 protein) and loops 29-34 and 108-128 of protein L5 could be visualized. Thus, this paper provides a supplemented version of the Hma 50S ribosomal subunit model.