1F7V

CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG

1F7V の概要

• エントリーDOI: 10.2210/pdb1f7v/pdb
• 関連するPDBエントリー: 1BS2 1F7U
• 分子名称: TRNA(ARG), ARGINYL-TRNA SYNTHETASE (3 entities in total)
• 機能のキーワード: trna-protein complex, aminoacylation, arginyl-trna synthetase, ligase-rna complex, ligase/rna
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94191.64

構造登録者

Delagoutte, B.,Moras, D.,Cavarelli, J. (登録日: 2000-06-28, 公開日: 2001-06-27, 最終更新日: 2024-02-07)

主引用文献

Delagoutte, B.,Moras, D.,Cavarelli, J.
tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
EMBO J., 19:5599-5610, 2000

PubMed Abstract: The 2.2 A crystal structure of a ternary complex formed by yeast arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the L-arginine substrate highlights new atomic features used for specific substrate recognition. This first example of an active complex formed by a class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA illustrates additional strategies used for specific tRNA selection. The enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop never seen before. Moreover, the anticodon binding triggers conformational changes in the catalytic center of the protein. The comparison with the 2.9 A structure of a binary complex formed by yeast arginyl-tRNA synthetase and tRNA(Arg) reveals that L-arginine binding controls the correct positioning of the CCA end of the tRNA(Arg). Important structural changes induced by substrate binding are observed in the enzyme. Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction.

PubMed: 11060012
DOI: 10.1093/emboj/19.21.5599

実験手法

X-RAY DIFFRACTION (2.9 Å)