3TEG

Bacterial and Eukaryotic Phenylalanyl-tRNA Synthetases Catalyze Misaminoacylation of tRNAPhe with 3,4-Dihydroxy-L-Phenylalanine (L-Dopa)

3TEG の概要

• エントリーDOI: 10.2210/pdb3teg/pdb
• 関連するPDBエントリー: 3CMQ 3HFV 3TEH
• 分子名称: Phenylalanyl-tRNA synthetase, mitochondrial, 3,4-DIHYDROXYPHENYLALANINE (3 entities in total)
• 機能のキーワード: dopa, l-dopa, trna, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix (Potential): O95363
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48703.23

構造登録者

Moor, N.,Klipcan, L.,Safro, M. (登録日: 2011-08-14, 公開日: 2011-11-23, 最終更新日: 2023-09-13)

主引用文献

Moor, N.,Klipcan, L.,Safro, M.G.
Bacterial and Eukaryotic Phenylalanyl-tRNA Synthetases Catalyze Misaminoacylation of tRNA(Phe) with 3,4-Dihydroxy-L-Phenylalanine.
Chem.Biol., 18:1221-1229, 2011

PubMed Abstract: Aminoacyl-tRNA synthetases exert control over the accuracy of translation by selective pairing the correct amino acids with their cognate tRNAs, and proofreading the misacylated products. Here we show that three existing, structurally different phenylalanyl-tRNA synthetases-human mitochondrial (HsmtPheRS), human cytoplasmic (HsctPheRS), and eubacterial from Thermus thermophilus (TtPheRS), catalyze mischarging of tRNA(Phe) with an oxidized analog of tyrosine-L-dopa. The lowest level of L-dopa discrimination over the cognate amino acid, exhibited by HsmtPheRS, is comparable to that of tyrosyl-tRNA synthetase. HsmtPheRS and TtPheRS complexes with L-dopa revealed in the active sites an electron density shaping this ligand. HsctPheRS and TtPheRS possessing editing activity are capable of hydrolyzing the exogenous L-dopa-tRNA(Phe) as efficiently as Tyr-tRNA(Phe). However, editing activity of PheRS does not guarantee reduction of the aminoacylation error rate to escape misincorporation of L-dopa into polypeptide chains.

PubMed: 22035791
DOI: 10.1016/j.chembiol.2011.08.008

実験手法

X-RAY DIFFRACTION (2.2044 Å)