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2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 17151Article in journal (Refereed) Published
Abstract [en]
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 angstrom 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.
Place, publisher, year, edition, pages
Nature Publishing Group, 2017
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-143523 (URN)10.1038/s41598-017-17044-3 (DOI)000417354200004 ()29215017 (PubMedID)2-s2.0-85038074530 (Scopus ID)
Note
The original version of this Article contained an error in the title of the paper, where “Anabaena sp. PCC 7120” was incorrectly given as “Anabaena sp. PCC 7210”. This has now been corrected in the PDF and HTML versions of the Article, and in the accompanying Supplementary Information file.
Errata: Author Correction: Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientifc reports. 2018;8:8658. DOI: 10.1038/s41598-018-26715-8
2018-01-042018-01-042018-06-15Bibliographically approved