Homology Modeling of tRNA-dependent Amidotransferase from Malaria Parasite

Abstract

Malaria is one of the most prevalent diseases in the world. The causative agent of malaria is a protozoan named Plasmodium. Many drugs have been invented against malaria parasite but increasing resistant against existing drugs necessitates the discovery of many new drugs. Plasmodium parasite is the member of apicomplexan group which harbor a plastid, apicoplast. The machinery of apicoplast protein synthesis is more like prokaryotic in nature. Hence, proteins involved in apicoplast functions are different from the host proteins and therefore these proteins could be targeted as possible and effective drug targets. Enzyme tRNA-dependent amidotransferase is present in the apicoplast and part of the alternate aminoacylation pathway for formation of Gln-tRNA^Gln. In this study, we have determined the structure of tRNA-dependent amidotransferase using homology modeling. Further, active site identification was also performed. These results will not only help in understanding the alternate pathway of aminoacylation in parasite but also lead to the development of new effective drugs against malaria.