8BHD

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

Summary for 8BHD

• Entry DOI: 10.2210/pdb8bhd/pdb
• Related: 8BCQ
• Descriptor: Glutamate--tRNA ligase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: 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)
• Biological source: Plasmodium berghei ANKA
• Total number of polymer chains: 5
• Total formula weight: 152584.36

Authors

Benas, P.,Jaramillo Ponce, J.R.,Legrand, P.,Frugier, M.,Sauter, C. (deposition date: 2022-10-31, release date: 2023-01-25, Last modification date: 2024-06-19)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.17 Å)