Structural highlights
Function
RNZ_BACSU Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pellegrini O, Nezzar J, Marchfelder A, Putzer H, Condon C. Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis. EMBO J. 2003 Sep 1;22(17):4534-43. PMID:12941704 doi:http://dx.doi.org/10.1093/emboj/cdg435
- ↑ 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
