7FG6

Crystal structure of the Tyrosyl-tRNA synthetase (TyrRS) in Nanoarchaeum equitans

7FG6 の概要

• エントリーDOI: 10.2210/pdb7fg6/pdb
• 分子名称: Tyrosine--tRNA ligase (2 entities in total)
• 機能のキーワード: tyrrs, ligase, trna synthetase
• 由来する生物種: Nanoarchaeum equitans Kin4-M
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43244.29

構造登録者

Noguchi, H.,Kamata, K.,Park, S.Y.,Tamura, K. (登録日: 2021-07-26, 公開日: 2021-09-08, 最終更新日: 2023-11-29)

主引用文献

Horikoshi, T.,Noguchi, H.,Umehara, T.,Mutsuro-Aoki, H.,Kurihara, R.,Noguchi, R.,Hashimoto, T.,Watanabe, Y.,Ando, T.,Kamata, K.,Park, S.Y.,Tamura, K.
Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus.
Biochem.Biophys.Res.Commun., 575:90-95, 2021

PubMed Abstract: tRNA of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA, was prepared. The I200R mutant tyrosylated not only wild-type tRNA but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites.

PubMed: 34461441
DOI: 10.1016/j.bbrc.2021.08.070

実験手法

X-RAY DIFFRACTION (2.8 Å)