Prx4 (peroxiredoxin 4) is the only peroxiredoxin located in the ER (endoplasmic reticulum) and a proposed scavenger for H2O2. In the present study, we solved crystal structures of human Prx4 in three different redox forms and characterized the reaction features of Prx4 with H2O2. Prx4 exhibits a toroid-shaped decamer constructed of five catalytic dimers. Structural analysis revealed conformational changes around helix α2 and the C-terminal reigon with a YF (Tyr-Phe) motif from the partner subunit, which are required for interchain disulfide formation between Cys87 and Cys208, a critical step of the catalysis. The structural explanation for the restricting role of the YF motif on the active site dynamics is provided in detail. Prx4 has a high reactivity with H2O2, but is susceptible to overoxidation and consequent inactivation by H2O2. Either deletion of the YF motif or dissociation into dimers decreased the susceptibility of Prx4 to overoxidation by increasing the flexibility of Cys87.
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Research Article|
December 14 2011
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4
Xi Wang;
Xi Wang
1
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
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Likun Wang;
Likun Wang
1
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
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Xi'e Wang;
Xi'e Wang
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
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Fei Sun;
Fei Sun
2
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
2Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Chih-chen Wang
Chih-chen Wang
2
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
2Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Publisher: Portland Press Ltd
Received:
February 28 2011
Revision Received:
August 29 2011
Accepted:
September 15 2011
Accepted Manuscript online:
September 15 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 441 (1): 113–118.
Article history
Received:
February 28 2011
Revision Received:
August 29 2011
Accepted:
September 15 2011
Accepted Manuscript online:
September 15 2011
Citation
Xi Wang, Likun Wang, Xi'e Wang, Fei Sun, Chih-chen Wang; Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. Biochem J 1 January 2012; 441 (1): 113–118. doi: https://doi.org/10.1042/BJ20110380
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