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Published April 10, 1998 | public
Journal Article

Crystal Structure and Evolution of a Transfer RNA Splicing Enzyme


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.

Additional Information

© 1998 American Association for the Advancement of Science. Received 10 December 1997; accepted 13 February 1998. We thank D. Graham and C. Woese for M. jannaschii genomic DNA, P. Bjorkman and D. Rees for their helpful discussions and generosity in sharing their equipment, C. M. Ogata for x-ray beam time allocation, F. T. Burling and S. Diana for assistance in data collection, R. Story and M. Saks for critical review of the manuscript, and other members of the Abelson laboratory for their advice and support. This work was supported by American Cancer Society grant NP802 and NIH Individual National Research Service Award F32 GM188930-01. PDB code for the coordinates is 1a79.

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