Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease
Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease
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DOI：
10.1016/j.febslet.2004.09.074
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发表时间：
2004-11-05
期刊：
影响因子：
3.5
通讯作者：
Ohgi, T
中科院分区：
文献类型：
--
作者：
Horio, T;Murai, M;Ohgi, T
ISG 20是一种干扰素诱导的抗病毒核糖核酸外切酶，作用于单链RNA，对单链DNA也有较小的活性。它属于DEDD核酸外切酶超家族的DEDDh组RNA酶。我们以1.9分辨率解析了人ISG 20与两个Mn 2+离子和尿苷5 '-单磷酸（UMP）复合的晶体结构。它的结构，包括活性位点的结构，与两种DEDDh-组DNA酶，大肠杆菌DNA聚合酶III的E：亚基和大肠杆菌的相应结构域非常相似。大肠杆菌外切核酸酶I，强烈表明其催化机制是相同的，这两个DNA酶。然而，ISG 20还具有独特的残基Met 14和Arg 53，以适应与UMP核糖的2 '-OH基团的氢键，并且这些残基可能是ISG 20对RNA底物的偏好的原因。(C)2004年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
ISG20 is an interferon-induced antiviral exoribonuelease that acts on single-stranded RNA and also has minor activity towards single-stranded DNA. It belongs to the DEDDh group of RNases of the DEDD exonuclease superfamily. We have solved the crystal structure of human ISG20 complexed with two Mn2+ ions and uridine 5'-monophosphate (UMP) at 1.9 resolution. Its structure, including that of the active site, is very similar to those of the corresponding domains of two DEDDh-group DNases, the E: subunit of Escherichia coli DNA polymerase III and E. coli exonuclease I, strongly suggesting that its catalytic mechanism is identical to that of the two DNases. However, ISG20 also has distinctive residues, Met14 and Arg53, to accommodate hydrogen bonds with the 2'-OH group of the UMP ribose, and these residues may be responsible for the preference of ISG20 for RNA substrates. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.