| Literature DB >> 16518398 |
Inés Li de la Sierra-Gallay1, Nathalie Mathy, Olivier Pellegrini, Ciarán Condon.
Abstract
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 tRNA(Thr), 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.Entities:
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Year: 2006 PMID: 16518398 DOI: 10.1038/nsmb1066
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369