1IL2

Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex

1IL2 の概要

• エントリーDOI: 10.2210/pdb1il2/pdb
• 分子名称: ASPARTYL TRANSFER RNA, ASPARTYL-TRNA SYNTHETASE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: protein-rna complex, ligase-rna complex, ligase/rna
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P21889
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 181472.11

構造登録者

Moulinier, L.,Eiler, S.,Eriani, G.,Gangloff, J.,Thierry, J.C.,Gabriel, K.,McClain, W.H.,Moras, D. (登録日: 2001-05-07, 公開日: 2001-09-28, 最終更新日: 2024-04-03)

主引用文献

Moulinier, L.,Eiler, S.,Eriani, G.,Gangloff, J.,Thierry, J.C.,Gabriel, K.,McClain, W.H.,Moras, D.
The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
EMBO J., 20:5290-5301, 2001

PubMed Abstract: The 2.6 A resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the terminal adenosine. The structure suggests that the acceptor stem regulates the loop movement through sugar phosphate backbone- protein interactions. Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism.

PubMed: 11566892
DOI: 10.1093/emboj/20.18.5290

実験手法

X-RAY DIFFRACTION (2.6 Å)