Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin.
Structure
; 20(3): 429-39, 2012 Mar 07.
Article
em En
| MEDLINE
| ID: mdl-22405002
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.
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
3_ND
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
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Schistosoma mansoni
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Modelos Moleculares
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Peroxirredoxinas
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Modelos Químicos
Limite:
Animals
Idioma:
En
Revista:
Structure
Ano de publicação:
2012
Tipo de documento:
Article