1H3N

Leucyl-tRNA synthetase from Thermus thermophilus complexed with a sulphamoyl analogue of leucyl-adenylate

1H3N の概要

• エントリーDOI: 10.2210/pdb1h3n/pdb
• 分子名称: LEUCYL-TRNA SYNTHETASE, LEUCINE, [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDRO-2-FURANYL]METHYL SULFAMATE, ... (6 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, class i aminoacyl-trna synthetase, atp + l-leucine + trna (leu) -> amp + ppi + l-leucyl-trna(leu), ligase
• 由来する生物種: THERMUS THERMOPHILUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 102066.65

構造登録者

Cusack, S.,Yaremchuk, A.,Tukalo, M. (登録日: 2002-09-11, 公開日: 2002-09-27, 最終更新日: 2024-05-08)

主引用文献

Cusack, S.,Yaremchuk, A.,Tukalo, M.
The 2A Structure of Leucyl-tRNA Synthetase and its Complex with a Leucyl-Adenylate Analogue
Embo J., 19:2351-, 2000

PubMed Abstract: Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large monomeric class I synthetases. Each contains a homologous insertion domain of approximately 200 residues, which is thought to permit them to hydrolyse ('edit') cognate tRNA that has been mischarged with a chemically similar but non-cognate amino acid. We describe the first crystal structure of a leucyl-tRNA synthetase, from the hyperthermophile Thermus thermophilus, at 2.0 A resolution. The overall architecture is similar to that of isoleucyl-tRNA synthetase, except that the putative editing domain is inserted at a different position in the primary structure. This feature is unique to prokaryote-like leucyl-tRNA synthetases, as is the presence of a novel additional flexibly inserted domain. Comparison of native enzyme and complexes with leucine and a leucyl- adenylate analogue shows that binding of the adenosine moiety of leucyl-adenylate causes significant conformational changes in the active site required for amino acid activation and tight binding of the adenylate. These changes are propagated to more distant regions of the enzyme, leading to a significantly more ordered structure ready for the subsequent aminoacylation and/or editing steps.

PubMed: 10811626
DOI: 10.1093/EMBOJ/19.10.2351

実験手法

X-RAY DIFFRACTION (2 Å)