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Publication Abstract from PubMed
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.
Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA.,Li de la Sierra-Gallay I, Mathy N, Pellegrini O, Condon C Nat Struct Mol Biol. 2006 Apr;13(4):376-7. Epub 2006 Mar 5. PMID:16518398[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Li de la Sierra-Gallay I, Mathy N, Pellegrini O, Condon C. Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA. Nat Struct Mol Biol. 2006 Apr;13(4):376-7. Epub 2006 Mar 5. PMID:16518398 doi:10.1038/nsmb1066
