Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition

被引：90

作者：

Fukunaga, R

Yokoyama, S ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Tokyo 113, Japan

[2] RIKEN, Genom Sci Ctr, Yokohama, Kanagawa 2300045, Japan

[3] RIKEN, Harima Inst SPring 8, Mikazuki, Hyogo 6795148, Japan

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 10期

基金：

日本学术振兴会;

关键词：

D O I：

10.1038/nsmb985

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：

Leucyl-tRNA synthetase (LeuRS) specifically recognizes the characteristic long variable arm and the discriminator base, A73, of tRNALeu in archaea and eukarya. The LeuRS 'editing domain' hydrolyzes misformed noncognate aminoacyl-tRNA. Here we report the crystal structure of the archaeal Pyrococcus horikoshii LeuRS-tRNA(Leu) complex. The protruding C-terminal domain of LeuRS specifically recognizes the bases at the tip of the long variable arm. The editing domain swings from its tRNA-free position to avoid clashing with the tRNA. Consequently the tRNA CCA end can bend and reach the aminoacylation active site. The tRNA 3' region assumes two distinct conformations that allow A73 to be specifically recognized in different ways. One conformation is the canonical 'aminoacylation state.' The other conformation seems to be the 'intermediate state,' where the misaminoacylated 3' end has partially relocated to the editing domain.

引用

页码：915 / 922

页数：8

共 36 条

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