6IPA

C-terminal EMAP II-like domain of p43 refined against twinned data

6IPA の概要

• エントリーDOI: 10.2210/pdb6ipa/pdb
• 分子名称: aminoacyl-tRNA synthetase-interacting multifunctional protein p43 (2 entities in total)
• 機能のキーワード: aimp1, emapii-like domain, plasmodium, rna binding protein
• 由来する生物種: Plasmodium vivax (malaria parasite P. vivax)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 91488.82

構造登録者

Manickam, Y.,Harlos, K.,Gupta, S.,Sharma, A. (登録日: 2018-11-02, 公開日: 2019-11-06, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.47 Å)