2BTE

Thermus thermophilus Leucyl-tRNA synthetase complexed with a tRNAleu transcript in the post-editing conformation and a post- transfer editing substrate analogue

2BTE の概要

• エントリーDOI: 10.2210/pdb2bte/pdb
• 関連するPDBエントリー: 1H3N 1OBC 1OBH 2BYT
• 分子名称: AMINOACYL-TRNA SYNTHETASE, TRNALEU TRANSCRIPT WITH ANTICODON CAG, ZINC ION, ... (9 entities in total)
• 機能のキーワード: ligase, class i aminoacyl-trna synthetase editing
• 由来する生物種: THERMUS THERMOPHILUS; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 260229.93

構造登録者

Cusack, S.,Tukalo, M.,Yaremchuk, A.,Fukunaga, R.,Yokoyama, S. (登録日: 2005-05-31, 公開日: 2005-09-15, 最終更新日: 2023-12-13)

主引用文献

Tukalo, M.,Yaremchuk, A.,Fukunaga, R.,Yokoyama, S.,Cusack, S.
The Crystal Structure of Leucyl-tRNA Synthetase Complexed with tRNA(Leu) in the Post-Transfer- Editing Conformation.
Nat.Struct.Mol.Biol., 12:923-, 2005

PubMed Abstract: Leucyl-tRNA synthetase (LeuRS) has a specific post-transfer editing activity directed against mischarged isoleucine and similar noncognate amino acids. We describe the post-transfer-editing and product complexes of Thermus thermophilus LeuRS (LeuRSTT) with tRNA(Leu) at 2.9- to 3.3-A resolution. In the post-transfer-editing configuration, A76 binds in the editing active site exactly as previously found for the adenosine moiety of a small-molecule editing-substrate analog. The 60 C-terminal residues of LeuRSTT, unseen in previous structures, fold into a compact domain flexibly linked to the rest of the molecule and interacting with the G19-C56 tertiary base pair of tRNA(Leu). LeuRS recognition of tRNA(Leu) depends essentially on tRNA shape rather than base-specific interactions. The structures show that considerable domain rotations, notably of the editing domain, accompany the tRNA-3' end dynamics associated successively with aminoacylation, post-transfer editing and product release.

PubMed: 16155583
DOI: 10.1038/NSMB986

実験手法

X-RAY DIFFRACTION (2.9 Å)