Structure of the L1 protuberance in the ribosome
Structure of the L1 protuberance in the ribosome
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DOI：
10.1038/nsb886
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发表时间：
2003-02-01
期刊：
影响因子：
--
通讯作者：
Nikonov, S
中科院分区：
文献类型：
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作者：
Nikulin, A;Eliseikina, I;Nikonov, S
50S核糖体亚基的L1突起与从E位点释放/处置脱酰基tRNA有关。该核糖体区域的明显流动性迄今为止阻碍了其在50S亚基或70S核糖体内的三维结构的准确测定。在这里，我们报道了来自Sulfolobus acidocalarius的核糖体蛋白L1与来自Thermus thermophilus的特定的55个核苷酸片段23S rRNA复合物在2.65埃分辨率下的晶体结构。这种结构填补了目前50S核糖体亚基模型的一个主要空白。L1和rRNA片段的构象与嗜热T. 70S核糖体的晶体学模型有很大的不同。将L1- rrna复合物结合到嗜热T. 70S核糖体和耐辐射球菌50S亚基的结构模型中，可以可靠地表示核糖体中大部分L1突起。
The L1 protuberance of the 50S ribosomal subunit is implicated in the release/disposal of deacylated tRNA from the E site. The apparent mobility of this ribosomal region has thus far prevented an accurate determination of its three-dimensional structure within either the 50S subunit or the 70S ribosome. Here we report the crystal structure at 2.65 Angstrom resolution of ribosomal protein L1 from Sulfolobus acidocaldarius in complex with a specific 55-nucleotide fragment of 23S rRNA from Thermus thermophilus. This structure fills a major gap in current models of the 50S ribosomal subunit. The conformations of L1 and of the rRNA fragment differ dramatically from those within the crystallographic model of the T. thermophilus 70S ribosome. Incorporation of the L1-rRNA complex into the structural models of the T. thermophilus 70S ribosome and the Deinococcus radiodurans 50S subunit gives a reliable representation of most of the L1 protuberance within the ribosome.