2AMC

Crystal structure of Phenylalanyl-tRNA synthetase complexed with L-tyrosine

2AMC の概要

• エントリーDOI: 10.2210/pdb2amc/pdb
• 関連するPDBエントリー: 1b70 1b7y 1eiy 1jjc 1pys 2aly
• 分子名称: Phenylalanyl-tRNA synthetase alpha chain, Phenylalanyl-tRNA synthetase beta chain, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: protein-amino acid complex, ligase
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P27001 P27002
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117158.78

構造登録者

Kotik-Kogan, O.,Moor, N.,Tworowski, D.,Safro, M. (登録日: 2005-08-09, 公開日: 2005-12-20, 最終更新日: 2024-12-25)

主引用文献

Kotik-Kogan, O.,Moor, N.,Tworowski, D.,Safro, M.
Structural Basis for Discrimination of L-Phenylalanine from L-Tyrosine by Phenylalanyl-tRNA Synthetase
Structure, 13:1799-1807, 2005

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful transfer of amino acids onto cognate tRNAs. Since chemical structures of various amino acids closely resemble each other, it is difficult to discriminate between them. Editing activity has been evolved by certain aaRSs to resolve the problem. In this study, we determined the crystal structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable tyrosyl-adenylate analog. The structures demonstrate plasticity of the synthetic site capable of binding substrates larger than phenylalanine and provide a structural basis for the proofreading mechanism. The editing site is localized at the B3/B4 interface, 35 A from the synthetic site. Glubeta334 plays a crucial role in the specific recognition of the Tyr moiety in the editing site. The tyrosyl-adenylate analog binds exclusively in the synthetic site. Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system.

PubMed: 16338408
DOI: 10.1016/j.str.2005.08.013

実験手法

X-RAY DIFFRACTION (2.7 Å)