1C0A

CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX

1C0A の概要

• エントリーDOI: 10.2210/pdb1c0a/pdb
• 分子名称: ASPARTYL TRNA, ASPARTYL TRNA SYNTHETASE, SULFATE ION, ... (6 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
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91339.35

構造登録者

Eiler, S.,Dock-Bregeon, A.-C.,Moulinier, L.,Thierry, J.-C.,Moras, D. (登録日: 1999-07-15, 公開日: 1999-11-23, 最終更新日: 2024-02-07)

主引用文献

Eiler, S.,Dock-Bregeon, A.,Moulinier, L.,Thierry, J.C.,Moras, D.
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.
EMBO J., 18:6532-6541, 1999

PubMed Abstract: The 2.4 A crystal structure of the Escherichia coli aspartyl-tRNA synthetase (AspRS)-tRNA(Asp)-aspartyl-adenylate complex shows the two substrates poised for the transfer of the aspartic acid moiety from the adenylate to the 3'-hydroxyl of the terminal adenosine of the tRNA. A general molecular mechanism is proposed for the second step of the aspartylation reaction that accounts for the observed conformational changes, notably in the active site pocket. The stabilization of the transition state is mediated essentially by two amino acids: the class II invariant arginine of motif 2 and the eubacterial-specific Gln231, which in eukaryotes and archaea is replaced by a structurally non-homologous serine. Two archetypal RNA-protein modes of interactions are observed: the anticodon stem-loop, including the wobble base Q, binds to the N-terminal beta-barrel domain through direct protein-RNA interactions, while the binding of the acceptor stem involves both direct and water-mediated hydrogen bonds in an original recognition scheme.

PubMed: 10562565
DOI: 10.1093/emboj/18.22.6532

実験手法

X-RAY DIFFRACTION (2.4 Å)