Structure of the ubiquitous 3′ processing enzyme RNase Z bound to transfer RNA
Structure of the ubiquitous 3′ processing enzyme RNase Z bound to transfer RNA
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DOI：
10.1038/nsmb1066
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发表时间：
2006-04-01
影响因子：
16.8
通讯作者：
Condon, C
中科院分区：
文献类型：
--
作者：
de la Sierra-Gallay, IL;Mathy, N;Condon, C
高度保守的核糖核酸酶RNase Z催化大多数tRNA前体的3'延伸的核内溶解去除。在这里，我们展示了枯草芽孢杆菌RNase Z和tRNAThr之间复合物的结构，tRNAThr是与tRNA结合的核糖核分解加工酶的第一个结构。tRNA与RNase Z结合会引起双方的构象变化，从而促进催化位点的重组和tRNA的裂解。
The highly conserved ribonuclease RNase Z catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Here we present the structure of the complex between Bacillus subtilis RNase Z and tRNAThr, the first structure of a ribonucleolytic processing enzyme bound to tRNA. Binding of tRNA to RNase Z causes conformational changes in both partners to promote reorganization of the catalytic site and tRNA cleavage.