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The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on <jats:italic>Leishmania infantum<\/jats:italic> mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein.<\/jats:p>","DOI":"10.1038\/s41467-019-08565-8","type":"journal-article","created":{"date-parts":[[2019,2,8]],"date-time":"2019-02-08T13:55:25Z","timestamp":1549634125000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":48,"title":["Chaperone activation and client binding of a 2-cysteine peroxiredoxin"],"prefix":"10.1038","volume":"10","author":[{"given":"Filipa","family":"Teixeira","sequence":"first","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2082-9006","authenticated-orcid":false,"given":"Eric","family":"Tse","sequence":"additional","affiliation":[]},{"given":"Helena","family":"Castro","sequence":"additional","affiliation":[]},{"given":"Karl A. 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