Journal
STRUCTURE
Volume 20, Issue 3, Pages 429-439Publisher
CELL PRESS
DOI: 10.1016/j.str.2012.01.004
Keywords
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Funding
- Fondazione Roma
- Sapienza University of Rome Ricerche Universitarie
- MIUR of Italy [2007-protRBRN07BMCT]
- National Institute of Allergy and Infectious Diseases [AI065622]
- European Community [226716]
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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 Prx1 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 H2O2 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.
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