FIGURE 1.

A ribbon representation of the TIM barrel fold from the predicted model structures of Chitinases from (a) Plasmodium falciparum and (b) Plasmodium vivax prepared by PyMOL. TIM Barrel is an eight stranded α‐β fold with β sheets forming a barrel (black), surrounded by α helices. Plasmodium falciparum chitinase contains a single catalytic domain (depicted in green and black comprising of α helices and β sheets, respectively). In Plasmodium vivax, the pro‐domain (red) and Chitin binding domain (orange) flanks the catalytic domain. (c) depicts the domain architecture of Plasmodium chitinases. Short form (PfCHT1, PgCHT2, PrCHT1, PreCHT2) and Long forms (PvCHT1, PgCHT1, PbCHT1, PreCHT1) of Plasmodium chitinases are annotated at the catalytic domain and chitin binding domains as reported elsewhere. ³¹ The signal sequence ranges from 1–20 (observed in the long form) to 1–31/32 residues (observed in PgCHT2, a representative of short form). Long form of chitinases harbor pro‐domain, catalytic domain, and chitin binding domain. Pro‐domain although not annotated in most cases, is found to be located at the N‐terminal end of the catalytic domain in PvCHT1 and PbCHT1. Represented chitinases are PgCHT1 and PgCHT2: Plasmodium gallinaceum chitinase, PfCHT1: Plasmodium falciparum chitinase, PvCHT1: Plasmodium vivax chitinase, PbCHT1: Plasmodium berghei chitinase, PrCHT1: Plasmodium reichenowei chitinase, PreCHT1 and PreCHT2: Plasmodium relictum chitinase