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 (CP) and, if present, the resolving Cys (CR). A detailed catalytic cycle has b...

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Autores principales:	Yogesh Mishra, Michael Hall, Roland Locmelis, Kwangho Nam, Christopher A. G. Söderberg, Patrik Storm, Neha Chaurasia, Lal Chand Rai, Stefan Jansson, Wolfgang P. Schröder, Uwe H. Sauer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6dd50dd40579437da29c2f089e3c0464
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spelling	oai:doaj.org-article:6dd50dd40579437da29c2f089e3c04642021-12-02T15:06:11ZActive-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 712010.1038/s41598-017-17044-32045-2322https://doaj.org/article/6dd50dd40579437da29c2f089e3c04642017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-17044-3https://doaj.org/toc/2045-2322Abstract 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.Yogesh MishraMichael HallRoland LocmelisKwangho NamChristopher A. G. SöderbergPatrik StormNeha ChaurasiaLal Chand RaiStefan JanssonWolfgang P. SchröderUwe H. SauerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yogesh Mishra Michael Hall Roland Locmelis Kwangho Nam Christopher A. G. Söderberg Patrik Storm Neha Chaurasia Lal Chand Rai Stefan Jansson Wolfgang P. Schröder Uwe H. Sauer Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
description	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 (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.
format	article
author	Yogesh Mishra Michael Hall Roland Locmelis Kwangho Nam Christopher A. G. Söderberg Patrik Storm Neha Chaurasia Lal Chand Rai Stefan Jansson Wolfgang P. Schröder Uwe H. Sauer
author_facet	Yogesh Mishra Michael Hall Roland Locmelis Kwangho Nam Christopher A. G. Söderberg Patrik Storm Neha Chaurasia Lal Chand Rai Stefan Jansson Wolfgang P. Schröder Uwe H. Sauer
author_sort	Yogesh Mishra
title	Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
title_short	Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
title_full	Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
title_fullStr	Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
title_full_unstemmed	Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
title_sort	active-site plasticity revealed in the asymmetric dimer of anprx6 the 1-cys peroxiredoxin and molecular chaperone from anabaena sp. pcc 7120
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6dd50dd40579437da29c2f089e3c0464
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Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120

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