3ZVJ

Crystal structure of high molecular weight (HMW) form of Peroxiredoxin I from Schistosoma mansoni

Summary for 3ZVJ

• Entry DOI: 10.2210/pdb3zvj/pdb
• Related: 3ZTL
• Descriptor: THIOREDOXIN PEROXIDASE (2 entities in total)
• Functional Keywords: oxidoreductase, schistosomiasis, chaperone, thioredoxin fold
• Biological source: SCHISTOSOMA MANSONI; More
• Total number of polymer chains: 20
• Total formula weight: 497042.18

Authors

Saccoccia, F.,Angelucci, F.,Bellelli, A.,Boumis, G.,Brunori, M.,Miele, A.E. (deposition date: 2011-07-25, release date: 2012-03-21, Last modification date: 2023-12-20)

Primary citation

Saccoccia, F.,Di Micco, P.,Boumis, G.,Brunori, M.,Koutris, I.,Miele, A.E.,Morea, V.,Sriratana, P.,Williams, D.L.,Bellelli, A.,Angelucci, F.
Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin.
Structure, 20:429-, 2012

PubMed 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.

PubMed: 22405002
DOI: 10.1016/J.STR.2012.01.004

Experimental method

X-RAY DIFFRACTION (3 Å)