Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein. Issue 2 (10th February 2020)

• Record Type: Journal Article
• Authors: Gupta, Swati; Chhibber-Goel, Jyoti; Sharma, Manmohan; Parvez, Suhel; Harlos, Karl; Sharma, Amit; Yogavel, Manickam
• Is Part Of: Acta crystallographica. Volume 76:Issue 2(2020)
• Page Start: 135
• Page End: 146
• Publication Date: 2020-02-10
• Subjects: aminoacyl‐tRNA synthetase interacting multifunctional proteins -- AIMPs -- crystal structure -- p43 -- Plasmodium vivax -- glutathione S‐transferase -- GST -- tRNA; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798319016413
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : Three non‐aminoacyl‐tRNA synthetase (aaRS) scaffold proteins, AIMP1/p43 (pro‐EMAP II), AIMP2/p38 and AIMP3/p18, known as aaRS‐interacting multifunctional proteins, are critical in driving the assembly of multi‐aaRS complexes in higher eukaryotes. Here, the structural features of the N‐ and C‐terminal domains of the Plasmodium vivax p43 ( Pv p43) protein are addressed. A comprehensive structural analyses of the two domains of Pv p43 reveals several notable features which suggest that it is likely to be a soluble, cytosolic protein with a dimeric assembly of its N‐terminal GST‐like domain that differs from canonical GST dimers. 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 ( 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.