Aminoacyl-tRNA synthetases: structural aspects of evolution and tRNA recognition

被引：15
|
作者：
Steitz, Thomas A. [1 ,2 ,3 ]
机构：
[1] Yale Univ, Howard Hughes Med Inst, New Haven, CT 06511 USA
[2] Yale Univ, Dept Mol Biophys, New Haven, CT 06511 USA
[3] Yale Univ, Dept Chem, New Haven, CT 06511 USA
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1991年 / 1卷 / 01期
关键词：
D O I：
10.1016/0959-440X(91)90022-L
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Structural studies of aminoacyl-tRNA synthetases have uncovered two strikingly different classes of synthetases that divide the twenty naturally occurring amino acids evenly between them. The glutaminyl-tRNA synthetase contacts the entire inside of the relevant L-shaped tRNA, making interactions that discriminate among tRNAs at the acceptor end and stem of the molecule, and in the anticodon loop.
引用
收藏
页码：139 / 143
页数：5
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