结核分枝杆菌核糖核酸酶III核酸酶结构域在2.1埃分辨率下的结构
Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 A.
作者信息
Akey David L, Berger James M
机构信息
Department of Molecular and Cellular Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
出版信息
Protein Sci. 2005 Oct;14(10):2744-50. doi: 10.1110/ps.051665905. Epub 2005 Sep 9.
Abstract
RNase III enzymes are a highly conserved family of proteins that specifically cleave double-stranded (ds)RNA. These proteins are involved in a diverse group of functions, including ribosomal RNA processing, mRNA maturation and decay, snRNA and snoRNA processing, and RNA interference. Here we report the crystal structure of the nuclease domain of RNase III from the pathogen Mycobacterium tuberculosis. Although globally similar to other RNase III folds, this structure has some features not observed in previously reported models. These include the presence of an additional metal ion near the catalytic site, as well as conserved secondary structural elements that are proposed to have functional roles in the recognition of dsRNAs.
摘要
核糖核酸酶III（RNase III）是一类高度保守的蛋白质家族，可特异性切割双链（ds）RNA。这些蛋白质参与多种功能，包括核糖体RNA加工、信使核糖核酸（mRNA）成熟与降解、小核RNA（snRNA）和小核仁RNA（snoRNA）加工以及RNA干扰。在此，我们报道了来自病原体结核分枝杆菌的RNase III核酸酶结构域的晶体结构。尽管该结构在整体上与其他RNase III折叠相似，但具有一些先前报道模型中未观察到的特征。这些特征包括催化位点附近存在一个额外的金属离子，以及一些保守的二级结构元件，这些元件被认为在双链RNA的识别中具有功能作用。
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