Crystal structure and evolution of a transfer RNA splicing enzyme

被引：124

作者：

Li, H ^{[1
]}

Trotta, CR ^{[1
]}

Abelson, J ^{[1
]}

机构：

[1] CALTECH, Div Biol, Pasadena, CA 91125 USA

来源：

SCIENCE | 1998年 / 280卷 / 5361期

关键词：

D O I：

10.1126/science.280.5361.279

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：279 / 284

页数：6

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[1] Structure of HIV-1 TAB RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge [J].