Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin

Structure. 2012 Mar 7;20(3):429-39. doi: 10.1016/j.str.2012.01.004.

Abstract

2-Cys peroxiredoxins (Prxs) play two different roles depending on the physiological status of the cell. They are thioredoxin-dependent peroxidases under low oxidative stress and ATP-independent chaperones upon exposure to high peroxide concentrations. These alternative functions have been associated with changes in the oligomerization state from low-(LMW) to high-molecular-weight (HMW) species. Here we present the structures of Schistosoma mansoni PrxI in both states: the LMW decamer and the HMW 20-mer formed by two stacked decamers. The latter is the structure of a 2-Cys Prx chaperonic form. Comparison of the structures sheds light on the mechanism by which chemical stressors, such as high H(2)O(2) concentration and acidic pH, are sensed and translated into a functional switch in this protein family. We also propose a model to account for the in vivo formation of long filaments of stacked Prx rings.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Chaperones / chemistry
  • Peroxidase / chemistry
  • Peroxiredoxins / chemistry*
  • Protein Conformation*
  • Schistosoma mansoni / chemistry*

Substances

  • Molecular Chaperones
  • Peroxiredoxins
  • Peroxidase

Associated data

  • PDB/3ZTL
  • PDB/3ZVJ