Structural highlights
Function
[ENDA_METJA] Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.[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 splicing of transfer RNA precursors is similar in Eucarya and Archaea. In both kingdoms an endonuclease recognizes the splice sites and releases the intron, but the mechanism of splice site recognition is different in each kingdom. The crystal structure of the endonuclease from the archaeon Methanococcus jannaschii was determined to a resolution of 2.3 angstroms. The structure indicates that the cleavage reaction is similar to that of ribonuclease A and the arrangement of the active sites is conserved between the archaeal and eucaryal enzymes. These results suggest an evolutionary pathway for splice site recognition.
Crystal structure and evolution of a transfer RNA splicing enzyme.,Li H, Trotta CR, Abelson J Science. 1998 Apr 10;280(5361):279-84. PMID:9535656[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lykke-Andersen J, Garrett RA. RNA-protein interactions of an archaeal homotetrameric splicing endoribonuclease with an exceptional evolutionary history. EMBO J. 1997 Oct 15;16(20):6290-300. PMID:9321408 doi:http://dx.doi.org/10.1093/emboj/16.20.6290
- ↑ Li H, Trotta CR, Abelson J. Crystal structure and evolution of a transfer RNA splicing enzyme. Science. 1998 Apr 10;280(5361):279-84. PMID:9535656
