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Fig. 1 | Malaria Journal

Fig. 1

From: Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study

Fig. 1

Key domains of aminoacyl tRNA synthetases. a Class I aaRS showing the Catalytic Domain (CD) and the anticodon binding domain (ABD). The CD has a CPI insert in all the proteins in this class. The CPI insert (orange) in IleRS, LeuRS and ValRS is enlarged to form an editing domain while in TyrRS and TrpRS it functions in the formation of dimers. ArgRS has an Add1 domain (cyan) at the N-terminus which is involved in tRNA recognition. b Class II aaRS showing the catalytic domain with the three conserved motifs (I, II and III). In GlyRS, HisRS and ProRS the anticodon binding domain is at the C-terminal. In AspRS, AsnRS and LysRS it is at the N-terminal, while in AspRS, LysRS and AsnRS proteins, the ABD occurs at the C-terminal. Dimer interfaces are shown by a magenta colour and are characterized by motif I. ProRS has an editing domain that occurs between motif I and II at the catalytic site while in ThrRS the editing domain is located at the N-terminal. AlaRS has a C-Ala domain (gold) at the C-terminal that functions in dimer formation [47]

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