2CV0

Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and L-glutamate

2CV0 の概要

• エントリーDOI: 10.2210/pdb2cv0/pdb
• 関連するPDBエントリー: 1G59 1GLN 1J09 1N75 1N77 1N78 2CUZ 2CV1 2CV2 2DXI
• 分子名称: tRNA, glutamyl-tRNA synthetase, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: ligase, rna, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, ligase-rna complex, ligase/rna
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P27000
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156530.99

構造登録者

Sekine, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-05-31, 公開日: 2006-09-05, 最終更新日: 2024-03-13)

主引用文献

Sekine, S.,Shichiri, M.,Bernier, S.,Chenevert, R.,Lapointe, J.,Yokoyama, S.
Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase
Structure, 14:1791-1799, 2006

PubMed Abstract: Glutamyl-tRNA synthetase (GluRS) is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation. We analyzed the role of tRNA in amino acid recognition by crystallography. In the GluRS*tRNA(Glu)*Glu structure, GluRS and tRNA(Glu) collaborate to form a highly complementary L-glutamate-binding site. This collaborative site is functional, as it is formed in the same manner in pretransition-state mimic, GluRS*tRNA(Glu)*ATP*Eol (a glutamate analog), and posttransition-state mimic, GluRS*tRNA(Glu)*ESA (a glutamyl-adenylate analog) structures. In contrast, in the GluRS*Glu structure, only GluRS forms the amino acid-binding site, which is defective and accounts for the binding of incorrect amino acids, such as D-glutamate and L-glutamine. Therefore, tRNA(Glu) is essential for formation of the completely functional binding site for L-glutamate. These structures, together with our previously described structures, reveal that tRNA plays a crucial role in accurate positioning of both L-glutamate and ATP, thus driving the amino acid activation.

PubMed: 17161369
DOI: 10.1016/j.str.2006.10.005

実験手法

X-RAY DIFFRACTION (2.4 Å)