Structure of the ubiquitous 3′ processing enzyme RNase Z bound to transfer RNA

被引：60

作者：

de la Sierra-Gallay, IL

Mathy, N

Pellegrini, O

Condon, C

机构：

[1] CNRS, FRC550, F-75005 Paris, France

[2] CNRS, UPR 9073, Inst Biol Phys Chim, F-75005 Paris, France

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 04期

关键词：

D O I：

10.1038/nsmb1066

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：376 / 377

页数：2

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