The structure of an AspRS-tRNAAsp complex reveals a tRNA-dependent control mechanism

被引：84

作者：

Moulinier, L

Eiler, S

Eriani, G

Gangloff, J

Thierry, JC

Gabriel, K

McClain, WH

Moras, D

机构：

[1] ULP, CNRS INSERM, Inst Genet & Biol Mol & Cellulaire, UPR 9004,Lab Biol & Genom Struct, F-67404 Illkirch Graffenstaden, France

[2] IBMC, UPR 9002, F-67084 Strasbourg, France

[3] Univ Wisconsin, Dept Bacteriol, Madison, WI 53706 USA

来源：

EMBO JOURNAL | 2001年 / 20卷 / 18期

关键词：

aminoacylation reaction; crystal structure; protein-RNA recognition; species specificity;

D O I：

10.1093/emboj/20.18.5290

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：

The 2.6 Angstrom resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the terminal adenosine. The structure suggests that the acceptor stem regulates the loop movement through sugar phosphate backbone-protein interactions. Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism.

引用

页码：5290 / 5301

页数：12

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