Inhibition of Schistosoma mansoni Thioredoxin-glutathione Reductase by Auranofin

Our results suggest a possible mechanism of inhibition of thiol-dependent reductases by AF, namely the transfer of gold(I) to one or more redox-active Cys couples of the enzyme

Francesco Angelucci; Ahmed A. Sayed; David L. Williams; Giovanna Boumis; Maurizio Brunori; Daniela Dimastrogiovanni; Adriana E. Miele; Frida Pauly; Andrea Bellelli

2009

Scholarcy highlights

  • Structure Refinement and Analysis—The structure was solved by molecular replacement using the program PHASER and the structure of truncated SmTGR as the search model
  • Ramachandran plot Most preferred Allowed Generously allowed a Highest resolution shell is shown in parentheses
  • Structural Analysis—The structure of wild type SmTGR treated with AF was solved by molecular replacement
  • Our data demonstrate that wild type SmTGR is inactivated by AF faster than both its truncated variant and yeast GR and an external source of selenium greatly speeds up the reactivity of Sec-free thiol reductases
  • The crystal contains 1 subunit/asymmetric unit, with a VM of 3.2 Å3 DaϪ1 and a solvent content of 61.3%

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