Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein

DOI: 10.1107/S2059798319016413

Authors: Swati Gupta (International Centre for Genetic Engineering and Biotechnology (ICGEB)) , Jyoti Chhibber-Goel (International Centre for Genetic Engineering and Biotechnology (ICGEB)) , Manmohan Sharma (International Centre for Genetic Engineering and Biotechnology (ICGEB); Jamia Hamdard University) , Suhel Parvez (Jamia Hamdard University) , Karl Harlos (Wellcome Centre for Human Genetics, University of Oxford) , Amit Sharma (International Centre for Genetic Engineering and Biotechnology (ICGEB)) , Manickam Yogavel (International Centre for Genetic Engineering and Biotechnology (ICGEB))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 76

State: Published (Approved)
Published: February 2020
Diamond Proposal Number(s): 14744

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.

Journal Keywords: aminoacyl-tRNA synthetase interacting multifunctional proteins; AIMPs; crystal structure; p43; Plasmodium vivax; glutathione S-transferase; GST; tRNA

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Added On: 06/02/2020 10:45

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)