Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing.
Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing.
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大肠杆菌 RNase D 的晶体结构，一种参与结构化 RNA 加工的核糖核酸外切酶。
DOI：
10.1016/j.str.2005.04.015
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Malhotra,Arun
中科院分区：
文献类型：
--
作者：
Zuo,Yuhong;Wang,Yong;Malhotra,Arun
RNase D (RND) is one of seven exoribonucleases identified inEscherichia coli. RNase D has homologs in many eubacteria and eukaryotes, and has been shown to contribute to the 3′ maturation of several stable RNAs. Here, we report the 1.6 Å resolution crystal structure ofE. coliRNase D. The conserved DEDD residues of RNase D fold into an arrangement very similar to the Klenow fragment exonuclease domain. Besides the catalytic domain, RNase D also contains two structurally similar α-helical domains with no discernible sequence homology between them. These closely resemble the HRDC domain previously seen in RecQ-family helicases and several other proteins acting on nucleic acids. More interestingly, the DEDD catalytic domain and the two helical domains come together to form a ring-shaped structure. The ring-shaped architecture ofE. coliRNase D and the HRDC domains likely play a major role in determining the substrate specificity of this exoribonuclease.
