Fig. 6

SNP profiles of cytoplasmic PfPRS. a Domain diagram of Plasmodium PRS. Aminoacylation, anticodon and zinc-binding domains are shown in pink, brown and peach respectively; the editing domain is shown in grey; and the disordered region in three-dimensional structures of PfPRS is shown as grey patterning. b The percentage distribution of amino acid mutations across the domains of PfPRS (left) and PvPRS (right). c The percentage frequency of amino acid mutations per domain in PfPRS and PvPRS [(total number of amino acid mutations divided by total number of residues in the enzyme) × 100]. d Structure of the PfPRS dimer surface (PDB ID: 4YDQ). For simplicity, the aminoacylation domain of only one monomer is coloured light pink. The two sequence patches of residues having no mutations (amino acids 291–368 [Patch 1] and amino acids 418–490 [Patch 2]) are shown in magenta and violet pink respectively. The substrate/drug binding pocket is indicated with a blue box. e Close-up view of the primary binding pocket of PfPRS bound with inhibitor halofuginone (magenta stick) and an ATP-analogue (orange stick). The proline and tRNA-binding pocket, which is occupied by halofuginone, is indicated in magenta. The ATP-binding pocket occupied by ATP-analog is indicated in yellow. The SNPs (green) are located > 8 Å from the primary binding pocket. Abbreviations: PvPRS P. vivax prolyl-tRNA synthetase