7WAO

Glutamyl-tRNA synthetase from Plasmodium falciparum (PfERS) in complex with Mn

7WAO の概要

• エントリーDOI: 10.2210/pdb7wao/pdb
• 分子名称: Glutamyl-tRNA synthetase, MANGANESE (II) ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: ers, glurs, glutamyl-trna synthetase, ligase, aminoacyl-trna synthetas, aminoacylation, manganese
• 由来する生物種: Plasmodium falciparum 3D7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61758.31

構造登録者

Sharma, V.,Manickam, Y.,Babbar, P.,Sharma, A. (登録日: 2021-12-14, 公開日: 2022-12-21, 最終更新日: 2023-11-29)

主引用文献

Sharma, V.K.,Chhibber-Goel, J.,Yogavel, M.,Sharma, A.
Structural characterization of glutamyl-tRNA synthetase (GluRS) from Plasmodium falciparum.
Mol.Biochem.Parasitol., 253:111530-111530, 2022

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes in protein translation machinery that provide the charged tRNAs needed for protein synthesis. Over the past decades, aaRSs have been studied as anti-parasitic, anti-bacterial, and anti-fungal drug targets. This study focused on the cytoplasmic glutamyl-tRNA synthetase (GluRS) from Plasmodium falciparum, which belongs to class Ib in aaRSs. GluRS unlike most other aaRSs requires tRNA to activate its cognate amino acid substrate L-Glutamate (L-Glu), and fails to form an intermediate adenylate complex in the absence of tRNA. The crystal structures of the Apo, ATP, and ADP-bound forms of Plasmodium falciparum glutamyl-tRNA synthetase (PfGluRS) were solved at 2.1 Å, 2.2 Å, and 2.8 Å respectively. The structural comparison of the Apo- and ATP-bound holo-forms of PfGluRS showed considerable conformational changes in the loop regions around the ATP-binding pocket of the enzyme. Biophysical characterization of the PfGluRS showed binding of the enzyme substrates L-Gluand ATP.. The sequence and structural conservation were evident across GluRS compared to other species. The structural dissection of the PfGluRS gives insight into the critical residues involved in the binding of ATP substrate, which can be harvested to develop new antimalarial drugs.

PubMed: 36370911
DOI: 10.1016/j.molbiopara.2022.111530

実験手法

X-RAY DIFFRACTION (2.582 Å)