1ZH6

Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine

1ZH6 の概要

• エントリーDOI: 10.2210/pdb1zh6/pdb
• 関連するPDBエントリー: 1ZH0
• 分子名称: Tyrosyl-tRNA synthetase, 4-ACETYL-L-PHENYLALANINE, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: structural plasticity, unnatural amino acid, trna synthetase, ketone, ligase
• 由来する生物種: Methanocaldococcus jannaschii
• 細胞内の位置: Cytoplasm: Q57834
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36463.41

構造登録者

Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G. (登録日: 2005-04-22, 公開日: 2006-04-04, 最終更新日: 2023-11-15)

主引用文献

Turner, J.M.,Graziano, J.,Spraggon, G.,Schultz, P.G.
Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase.
J.Am.Chem.Soc., 127:14976-14977, 2005

PubMed Abstract: It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acid p-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.

PubMed: 16248607
DOI: 10.1021/ja0549042

実験手法

X-RAY DIFFRACTION (2.5 Å)