1EQR

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

1EQR の概要

• エントリーDOI: 10.2210/pdb1eqr/pdb
• 関連するPDBエントリー: 1C0A
• 分子名称: ASPARTYL-TRNA SYNTHETASE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: domains, anti-parallel beta strand, beta barrel, oligomer binding fold, ligase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 198061.85

構造登録者

Rees, B.,Webster, G.,Delarue, M.,Boeglin, M.,Moras, D. (登録日: 2000-04-06, 公開日: 2000-06-29, 最終更新日: 2024-04-03)

主引用文献

Rees, B.,Webster, G.,Delarue, M.,Boeglin, M.,Moras, D.
Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates.
J.Mol.Biol., 299:1157-1164, 2000

PubMed Abstract: The crystal structure of aspartyl-tRNA synthetase from Escherichia coli has been determined to a resolution of 2.7 A. The structure is compared to the same enzyme co-crystallized with tRNA(Asp) and containing aspartyl adenylate or ATP. The asymmetric unit contains three monomers of the enzyme. While most parts of the protein show no significant differences in the three monomers, a few regions cannot be superimposed. Those regions are characterized by a high B-factor, and consist mostly of loops that make contacts with the tRNA in the complexes. The flexibility of the protein is seen at a global level, by the observation of a 10 to 15 degrees rotation of the N-terminal and insertion domains upon tRNA binding, and at the level of the individual amino acid residues, by main-chain and side-chain rearrangements. In contrast to these induced-fit conformational changes, a few residues essential for the tRNA anticodon or aspartyl-adenylate recognition exist in a predefined conformation, ensured by specific interactions within the protein.

PubMed: 10873442
DOI: 10.1006/jmbi.2000.3792

実験手法

X-RAY DIFFRACTION (2.7 Å)