Crystal structure of the specificity domain of ribonuclease P
Crystal structure of the specificity domain of ribonuclease P
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DOI：
10.1038/nature01386
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发表时间：
2003-02-13
期刊：
影响因子：
64.8
通讯作者：
Mondragón, A
中科院分区：
文献类型：
--
作者：
Krasilnikov, AS;Yang, XJ;Mondragón, A
RNase P是负责通过切割前体并导致tRNA成熟来加工转移RNA的5'末端的唯一内切核酸酶（1，2）。它含有RNA成分和蛋白质成分，并已在所有生物体中鉴定。它是最早被发现的催化性RNA之一，也是第一个在体内充当多重转换酶的RNA。核糖核酸酶P和核糖体是迄今为止已知的在所有生命王国中保守的仅有的两种核酶。细菌RNase P的RNA组分可以在体外不存在RNase P蛋白的情况下催化前体tRNA切割，并且由两个结构域组成：特异性结构域和催化结构域（4，5）。在这里，我们报告了枯草芽孢杆菌RNase P的154个核苷酸特异性结构域的3.15埃分辨率晶体结构。该结构揭示了该结构域的结构，维持分子整体折叠的相互作用，在所有RNase P RNA中保守的大的非螺旋但结构良好的模块，以及参与与底物相互作用的区域。
RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation(1,2). It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified(3) nd the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain(4,5). Here we report a 3.15-Angstrom resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.