5ZKF

Crystal Structure of N-terminal Domain of Plasmodium vivax p43 in space group P21

Summary for 5ZKF

• Entry DOI: 10.2210/pdb5zkf/pdb
• Descriptor: Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein p43 (2 entities in total)
• Functional Keywords: gst-like domain, aimp1, plasmodium, ligase
• Biological source: Plasmodium vivax (malaria parasite P. vivax)
• Total number of polymer chains: 4
• Total formula weight: 87245.12

Authors

Gupta, S.,Sharma, M.,Harlos, K.,Manickam, Y.,Sharma, A. (deposition date: 2018-03-23, release date: 2019-04-24, Last modification date: 2025-04-09)

Primary citation

Gupta, S.,Chhibber-Goel, J.,Sharma, M.,Parvez, S.,Harlos, K.,Sharma, A.,Yogavel, M.
Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein.
Acta Crystallogr D Struct Biol, 76:135-146, 2020

PubMed Abstract: Scaffold modules known as aminoacyl-tRNA synthetase (aaRS)-interacting multifunctional proteins (AIMPs), such as AIMP1/p43, AIMP2/p38 and AIMP3/p18, are important in driving the assembly of multi-aaRS (MARS) complexes in eukaryotes. Often, AIMPs contain an N-terminal glutathione S-transferase (GST)-like domain and a C-terminal OB-fold tRNA-binding domain. Recently, the apicomplexan-specific Plasmodium falciparum p43 protein (Pfp43) has been annotated as an AIMP and its tRNA binding, tRNA import and membrane association have been characterized. The crystal structures of both the N- and C-terminal domains of the Plasmodium vivax p43 protein (Pvp43), which is an ortholog of Pfp43, have been resolved. Analyses reveal the overall oligomeric structure of Pvp43 and highlight several notable features that show Pvp43 to be a soluble, cytosolic protein. The dimeric assembly of the N-terminal GST-like domain of Pvp43 differs significantly from canonical GST dimers, and it is tied to the C-terminal tRNA-binding domain via a linker region. This work therefore establishes a framework for dissecting the additional roles of p43 orthologs in eukaryotic multi-protein MARS complexes.

PubMed: 32038044
DOI: 10.1107/S2059798319016413

Experimental method

X-RAY DIFFRACTION (2.75 Å)