8BHD

N-terminal domain of Plasmodium berghei glutamyl-tRNA synthetase (Tbxo4 derivative crystal structure)

8BHD の概要

• エントリーDOI: 10.2210/pdb8bhd/pdb
• 関連するPDBエントリー: 8BCQ
• 分子名称: Glutamate--tRNA ligase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, trna, rna binding protein, protein complex, cell surface protein, multi-aminoacyl-trna synthetase complex (mars-msc), gst-like domain, aminoacyl-trna synthetase-interacting multifunctional proteins (aimp)
• 由来する生物種: Plasmodium berghei ANKA
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 152584.36

構造登録者

Benas, P.,Jaramillo Ponce, J.R.,Legrand, P.,Frugier, M.,Sauter, C. (登録日: 2022-10-31, 公開日: 2023-01-25, 最終更新日: 2024-06-19)

主引用文献

Jaramillo Ponce, J.R.,Theobald-Dietrich, A.,Benas, P.,Paulus, C.,Sauter, C.,Frugier, M.
Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.
Protein Sci., 32:e4564-e4564, 2023

PubMed Abstract: tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl-tRNA synthetases (aaRS), the glutamyl- (ERS), glutaminyl- (QRS), and methionyl- (MRS) tRNA synthetases. In eukaryotes, such multi-aaRSs complexes (MSC) regulate the moonlighting activities of aaRSs. In Plasmodium, tRip and the three aaRSs all contain an N-terminal GST-like domain involved in the assembly of two independent complexes: the Q-complex (tRip:ERS:QRS) and the M-complex (tRip:ERS:MRS) with a 2:2:2 stoichiometry and in which the association of the GST-like domains of tRip and ERS (tRip-N:ERS-N) is central. In this study, the crystal structure of the N-terminal GST-like domain of ERS was solved and made possible further investigation of the solution architecture of the Q- and M-complexes by small-angle x-ray scattering (SAXS). This strategy relied on the engineering of a tRip-N-ERS-N chimeric protein to study the structural scaffold of both Plasmodium MSCs and confirm the unique homodimerization pattern of tRip in solution. The biological impact of these structural arrangements is discussed.

PubMed: 36606712
DOI: 10.1002/pro.4564

実験手法

X-RAY DIFFRACTION (3.17 Å)