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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface.
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Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface.

机译:结构的核糖体蛋白L1产甲烷球菌属thermolithotrophicus。在L1重要结构不变量表面。

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摘要

The crystal structure of ribosomal protein L1 from the archaeon Methanococcus thermolithotrophicus has been determined at 2.7 A 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 A 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 A. 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.
机译:核糖体蛋白L1的晶体结构已经确定在2.7一项决议。水晶属于空间群P2 (1) 2 (1) 2 (1),晶胞参数= 67.0,b = 70.1, c =106.3 A和两个分子不对称单位。解决了结构爱茉莉和molecular-replacement方法精制与中枢神经系统的R值和一个18.9%R(免费)25.4%的分辨率范围30 - 2.7这个结构与比较获得以前两L1蛋白其他来源(栖热菌属的细菌的酸奶和archaeon m . jannaschii)以及详细分析分子间的联系相应的L1晶体结构不变量的分子表面可能重要的绑定23 s核糖体在核糖体RNA和蛋白质功能。

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