Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: Observation of the catalytic loop in the open conformation in the ligand-bound state

Abstract

Structures of triosephosphate isomerase (TIM) from the malarial parasite P. falciparum (Pf) complexed to the substrate analogues 3-phosphoglycerate and glycerol-3-phosphate have been determined at 2.4 Å resolution. The catalytic loop of TIM adopts a novel 'loop-open' conformation in these complexes. These structures provide insight into the design of inhibitors specific for the malarial enzyme.