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Title: Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120

Abstract

Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (C P) and, if present, the resolving Cys (C R). A detailed catalytic cycle has been derived for typical 2-Cys Prxs, however, little is known about the catalytic cycle of 1-Cys Prxs. We have characterized Prx6 from the cyanobacterium Anabaena sp. strain PCC7120 (AnPrx6) and found that in addition to the expected peroxidase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to other Prxs. The AnPrx6 crystal structure at 2.3 Å resolution reveals different active site conformations in each monomer of the asymmetric obligate homo-dimer. Molecular dynamic simulations support the observed structural plasticity. A FSH motif, conserved in 1-Cys Prxs, precedes the active site PxxxTxxCp signature and might contribute to the 1-Cys Prx reaction cycle.

Authors:
 [1];  [2];  [2];  [3];  [4];  [2];  [5];  [6];  [7];  [1];  [8]
  1. Umea Univ. (Sweden). Dept. of Chemistry and Umea Plant Science Center
  2. Umea Univ. (Sweden). Dept. of Chemistry
  3. Umea Univ. (Sweden). Dept. of Chemistry and Computational Life-Science Cluster (CLiC); Univ. of Texas, Arlington, TX (United States). Dept. of Chemistry and Biochemistry
  4. Lund Univ. (Sweden). MAX IV Lab.
  5. North Eastern Hill Univ., Shillong (India). Dept. of Biotechnology and Bioinformatics
  6. Banaras Hindu Univ, Varanasi (India). Molecular Biology Section
  7. Umea Univ. (Sweden). Umea Plant Science Center
  8. Umea Univ. (Sweden). Dept. of Chemistry and Computational Life-Science Cluster (CLiC)
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center
Sponsoring Org.:
USDOE
OSTI Identifier:
1490797
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Scientific Reports
Additional Journal Information:
Journal Volume: 7; Journal Issue: 1; Journal ID: ISSN 2045-2322
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Mishra, Yogesh, Hall, Michael, Locmelis, Roland, Nam, Kwangho, Söderberg, Christopher A. G., Storm, Patrik, Chaurasia, Neha, Rai, Lal Chand, Jansson, Stefan, Schröder, Wolfgang P., and Sauer, Uwe H. Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. United States: N. p., 2017. Web. doi:10.1038/s41598-017-17044-3.
Mishra, Yogesh, Hall, Michael, Locmelis, Roland, Nam, Kwangho, Söderberg, Christopher A. G., Storm, Patrik, Chaurasia, Neha, Rai, Lal Chand, Jansson, Stefan, Schröder, Wolfgang P., & Sauer, Uwe H. Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. United States. doi:10.1038/s41598-017-17044-3.
Mishra, Yogesh, Hall, Michael, Locmelis, Roland, Nam, Kwangho, Söderberg, Christopher A. G., Storm, Patrik, Chaurasia, Neha, Rai, Lal Chand, Jansson, Stefan, Schröder, Wolfgang P., and Sauer, Uwe H. Thu . "Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120". United States. doi:10.1038/s41598-017-17044-3. https://www.osti.gov/servlets/purl/1490797.
@article{osti_1490797,
title = {Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120},
author = {Mishra, Yogesh and Hall, Michael and Locmelis, Roland and Nam, Kwangho and Söderberg, Christopher A. G. and Storm, Patrik and Chaurasia, Neha and Rai, Lal Chand and Jansson, Stefan and Schröder, Wolfgang P. and Sauer, Uwe H.},
abstractNote = {Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (CP) and, if present, the resolving Cys (CR). A detailed catalytic cycle has been derived for typical 2-Cys Prxs, however, little is known about the catalytic cycle of 1-Cys Prxs. We have characterized Prx6 from the cyanobacterium Anabaena sp. strain PCC7120 (AnPrx6) and found that in addition to the expected peroxidase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to other Prxs. The AnPrx6 crystal structure at 2.3 Å resolution reveals different active site conformations in each monomer of the asymmetric obligate homo-dimer. Molecular dynamic simulations support the observed structural plasticity. A FSH motif, conserved in 1-Cys Prxs, precedes the active site PxxxTxxCp signature and might contribute to the 1-Cys Prx reaction cycle.},
doi = {10.1038/s41598-017-17044-3},
journal = {Scientific Reports},
issn = {2045-2322},
number = 1,
volume = 7,
place = {United States},
year = {2017},
month = {12}
}

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Works referenced in this record:

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