1TJE

Crystal structure of the editing domain of threonyl-tRNA synthetase

1TJE の概要

• エントリーDOI: 10.2210/pdb1tje/pdb
• 関連するPDBエントリー: 1QF6 1tke 1tkg 1tky
• 分子名称: Threonyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A8M3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25465.93

構造登録者

Dock-Bregeon, A.C.,Rees, B.,Torres-Larios, A.,Bey, G.,Caillet, J.,Moras, D. (登録日: 2004-06-04, 公開日: 2004-11-30, 最終更新日: 2023-08-23)

主引用文献

Dock-Bregeon, A.C.,Rees, B.,Torres-Larios, A.,Bey, G.,Caillet, J.,Moras, D.
Achieving Error-Free Translation; The Mechanism of Proofreading of Threonyl-tRNA Synthetase at Atomic Resolution.
Mol.Cell, 16:375-386, 2004

PubMed Abstract: The fidelity of aminoacylation of tRNA(Thr) by the threonyl-tRNA synthetase (ThrRS) requires the discrimination of the cognate substrate threonine from the noncognate serine. Misacylation by serine is corrected in a proofreading or editing step. An editing site has been located 39 A away from the aminoacylation site. We report the crystal structures of this editing domain in its apo form and in complex with the serine product, and with two nonhydrolyzable analogs of potential substrates: the terminal tRNA adenosine charged with serine, and seryl adenylate. The structures show how serine is recognized, and threonine rejected, and provide the structural basis for the editing mechanism, a water-mediated hydrolysis of the mischarged tRNA. When the adenylate analog binds in the editing site, a phosphate oxygen takes the place of one of the catalytic water molecules, thereby blocking the reaction. This rules out a correction mechanism that would occur before the binding of the amino acid on the tRNA.

PubMed: 15525511
DOI: 10.1016/j.molcel.2004.10.002

実験手法

X-RAY DIFFRACTION (1.5 Å)