Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus.: Functionally important structural invariants on the L1 surface
Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus.: Functionally important structural invariants on the L1 surface
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DOI：
10.1107/s0907444902006157
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发表时间：
2002-06-01
影响因子：
2.2
通讯作者：
Nikonov, S
中科院分区：
文献类型：
--
作者：
Nevskaya, N;Tishchenko, S;Nikonov, S
在2.7埃分辨率下测定了来自古菌嗜热嗜石甲烷球菌的核糖体蛋白L1的晶体结构。晶体属于空间群P2（1）2（1）2（1），晶胞参数a = 67.0，B = 70.1，c = 106.3埃，每个不对称单元有两个分子。通过用AMoRe的分子置换法解析结构，并用CNS精制，在30-2.7埃的分辨率范围内，R值为18.9%，无R值为25.4%。将这种结构与先前从其他来源（嗜热栖热菌和古菌M. jannaschii）以及对相应L1晶体中分子间接触的详细分析揭示了分子表面上的结构不变量，这些结构不变量可能对结合23 S核糖体RNA和核糖体内的蛋白质功能很重要。
The crystal structure of ribosomal protein L1 from the archaeon Methanococcus thermolithotrophicus has been determined at 2.7 Angstrom resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 70.1, c = 106.3 Angstrom and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with CNS to an R value of 18.9% and an R-free of 25.4% in the resolution range 30-2.7 Angstrom. Comparison of this structure with those obtained previously for two L1 proteins from other sources (the bacterium Thermus thermophilus and the archaeon M. jannaschii) as well as detailed analysis of intermolecular contacts in the corresponding L1 crystals reveal structural invariants on the molecular surface which are probably important for binding the 23S ribosomal RNA and protein function within the ribosome.