3ZVJ: Crystal Structure Of High Molecular Weight (Hmw) Form Of Peroxiredoxin I From Schistosoma Mansoni

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.
PDB ID: 3ZVJDownload
MMDB ID: 98216
PDB Deposition Date: 2011/7/25
Updated in MMDB: 2012/03
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 3ZVJ: eicosameric; determined by author and by software (PISA)
Molecular Components in 3ZVJ
Label Count Molecule
Proteins (20 molecules)
Thioredoxin Peroxidase
Molecule annotation
Thioredoxin Peroxidase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB