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Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stressMitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress
Structural highlights
Publication Abstract from PubMedMany 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum 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. Chaperone activation and client binding of a 2-cysteine peroxiredoxin.,Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomas AM, Southworth DR, Jakob U Nat Commun. 2019 Feb 8;10(1):659. doi: 10.1038/s41467-019-08565-8. PMID:30737390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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