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Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein
Author(s) -
Gupta Swati,
Chhibber-Goel Jyoti,
Sharma Manmohan,
Parvez Suhel,
Harlos Karl,
Sharma Amit,
Yogavel Manickam
Publication year - 2020
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319016413
Subject(s) - transfer rna , aminoacyl trna synthetase , linker , biology , microbiology and biotechnology , plasmodium falciparum , cytosol , amino acid , biochemistry , rna , enzyme , gene , malaria , computer science , immunology , operating system
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 ( Pf p43) 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 ( Pv p43), which is an ortholog of Pf p43, have been resolved. Analyses reveal the overall oligomeric structure of Pv p43 and highlight several notable features that show Pv p43 to be a soluble, cytosolic protein. The dimeric assembly of the N‐terminal GST‐like domain of Pv p43 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.