Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.

Highlights: [•] Two crystal structures of Plasmodium falciparum cytosolic TrpRS are reported. [•] The ligand-free protein undergoes conformational changes upon product formation. [•] Multiple residues collapse onto the active site when the product is bound. [•] The conformational changes are not completely replicated in human cytosolic TrpRS. [•] Molecules perturbing these changes could be useful for developing an anti-malaria drug. [Copyright &y& Elsevier]