Structure of the ubiquitous 3′ processing enzyme RNase Z bound to transfer RNA
- 5 March 2006
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 13 (4), 376-377
- https://doi.org/10.1038/nsmb1066
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 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.Keywords
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