8FZR

CryoEM structure of yeast Arginyltransferase 1 (ATE1)

8FZR の概要

• エントリーDOI: 10.2210/pdb8fzr/pdb
• EMDBエントリー: 29638
• 分子名称: Arginyl-tRNA--protein transferase 1, Arg tRNA, ZINC ION (3 entities in total)
• 機能のキーワード: arginyltransferase, post-translational modification, enzyme, transferase-rna complex, transferase/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: 82856.42

構造登録者

Huang, W.,Zhang, Y.,Taylor, D.J. (登録日: 2023-01-29, 公開日: 2023-04-26, 最終更新日: 2025-05-28)

主引用文献

Abeywansha, T.,Huang, W.,Ye, X.,Nawrocki, A.,Lan, X.,Jankowsky, E.,Taylor, D.J.,Zhang, Y.
The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.
Nat Commun, 14:2232-2232, 2023

PubMed Abstract: Arginyl-tRNA-protein transferase 1 (ATE1) is a master regulator of protein homeostasis, stress response, cytoskeleton maintenance, and cell migration. The diverse functions of ATE1 arise from its unique enzymatic activity to covalently attach an arginine onto its protein substrates in a tRNA-dependent manner. However, how ATE1 (and other aminoacyl-tRNA transferases) hijacks tRNA from the highly efficient ribosomal protein synthesis pathways and catalyzes the arginylation reaction remains a mystery. Here, we describe the three-dimensional structures of Saccharomyces cerevisiae ATE1 with and without its tRNA cofactor. Importantly, the putative substrate binding domain of ATE1 adopts a previously uncharacterized fold that contains an atypical zinc-binding site critical for ATE1 stability and function. The unique recognition of tRNA by ATE1 is coordinated through interactions with the major groove of the acceptor arm of tRNA. Binding of tRNA induces conformational changes in ATE1 that helps explain the mechanism of substrate arginylation.

PubMed: 37076488
DOI: 10.1038/s41467-023-38004-8

実験手法

ELECTRON MICROSCOPY (3.6 Å)