1EVL

CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE WITH A THREONYL ADENYLATE ANALOG

1EVL の概要

• エントリーDOI: 10.2210/pdb1evl/pdb
• 関連するPDBエントリー: 1EVK 1QF6
• 分子名称: THREONYL-TRNA SYNTHETASE, ZINC ION, 5'-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE, ... (4 entities in total)
• 機能のキーワード: amino acid recognition, zinc ion, trna-synthetase, adenylate analog, deletion mutant, ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A8M3
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 188952.05

構造登録者

Sankaranarayanan, R.,Dock-Bregeon, A.C.,Rees, B.,Moras, D. (登録日: 2000-04-20, 公開日: 2000-07-19, 最終更新日: 2024-02-07)

主引用文献

Sankaranarayanan, R.,Dock-Bregeon, A.C.,Rees, B.,Bovee, M.,Caillet, J.,Romby, P.,Francklyn, C.S.,Moras, D.
Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
Nat.Struct.Biol., 7:461-465, 2000

PubMed Abstract: Accurate translation of the genetic code depends on the ability of aminoacyl-tRNA synthetases to distinguish between similar amino acids. In order to investigate the basis of amino acid recognition and to understand the role played by the zinc ion present in the active site of threonyl-tRNA synthetase, we have determined the crystal structures of complexes of an active truncated form of the enzyme with a threonyl adenylate analog or threonine. The zinc ion is directly involved in threonine recognition, forming a pentacoordinate intermediate with both the amino group and the side chain hydroxyl. Amino acid activation experiments reveal that the enzyme shows no activation of isosteric valine, and activates serine at a rate 1,000-fold less than that of cognate threonine. This study demonstrates that the zinc ion is neither strictly catalytic nor structural and suggests how the zinc ion ensures that only amino acids that possess a hydroxyl group attached to the beta-position are activated.

PubMed: 10881191
DOI: 10.1038/75856

実験手法

X-RAY DIFFRACTION (1.55 Å)