Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site.

ABSTRACT: Pteridine reductase (PTR1) is a potential target for drug development against parasitic Trypanosoma and Leishmania species, protozoa that are responsible for a range of serious diseases found in tropical and subtropical parts of the world. As part of a structure-based approach to inhibitor development, specifically targeting Leishmania species, well ordered crystals of L. donovani PTR1 were sought to support the characterization of complexes formed with inhibitors. An efficient system for recombinant protein production was prepared and the enzyme was purified and crystallized in an orthorhombic form with ammonium sulfate as the precipitant. Diffraction data were measured to 2.5 Å resolution and the structure was solved by molecular replacement. However, a sulfate occupies a phosphate-bindi

SUBMITTER: Barrack KL 

PROVIDER: S-EPMC3079966 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature