7WAI
Glutamyl-tRNA synthetase from Plasmodium falciparum (PfERS)
Summary for 7WAI
| Entry DOI | 10.2210/pdb7wai/pdb |
| Descriptor | Glutamyl-tRNA synthetase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | ers, glurs, glutamyl-trna synthetase, ligase, aminoacyl-trna synthetas, aminoacylation |
| Biological source | Plasmodium falciparum 3D7 |
| Total number of polymer chains | 1 |
| Total formula weight | 61506.57 |
| Authors | Sharma, V.,Manickam, Y.,Harlos, K.,Sharma, A. (deposition date: 2021-12-14, release date: 2022-12-21, Last modification date: 2023-11-29) |
| Primary citation | 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 Cited by 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: 36370911DOI: 10.1016/j.molbiopara.2022.111530 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.105 Å) |
Structure validation
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