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http://purl.uniprot.org/citations/27238969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27238969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27238969http://www.w3.org/2000/01/rdf-schema#comment"Peroxiredoxins are antioxidant proteins primarily responsible for detoxification of hydroperoxides in cells. On exposure to various cellular stresses, peroxiredoxins can acquire chaperone activity, manifested as quaternary reorganization into a high molecular weight (HMW) form. Acidification, for example, causes dodecameric rings of human peroxiredoxin 3 (HsPrx3) to stack into long helical filaments. In this work, a 4.1-Å resolution structure of low-pH-instigated helical filaments was elucidated, showing a locally unfolded active site and partially folded C terminus. A 2.8-Å crystal structure of HsPrx3 was determined at pH 8.5 under reducing conditions, wherein dodecameric rings are arranged as a short stack, with symmetry similar to low-pH filaments. In contrast to previous observations, the crystal structure displays both a fully folded active site and ordered C terminus, suggesting that the HsPrx3 HMW form maintains catalytic activity. We propose a new role for the HMW form as a self-chaperoning assembly maintaining HsPrx3 function under stress."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2016.04.013"xsd:string
http://purl.uniprot.org/citations/27238969http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2016.04.013"xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Gerrard J.A."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Gerrard J.A."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Desfosses A."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Desfosses A."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Venugopal H."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Venugopal H."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Goldstone D.C."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Goldstone D.C."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Mitra A.K."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Mitra A.K."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Radjainia M."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Radjainia M."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Yosaatmadja Y."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Yosaatmadja Y."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Abrishami V."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Abrishami V."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Hampton M.B."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Hampton M.B."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Yewdall N.A."xsd:string
http://purl.uniprot.org/citations/27238969http://purl.uniprot.org/core/author"Yewdall N.A."xsd:string