6E0F

Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress

Summary for 6E0F

• Entry DOI: 10.2210/pdb6e0f/pdb
• Related: 6E0G
• EMDB information: 8946 8947
• Descriptor: mitochondrial 2-cys-peroxiredoxin (1 entity in total)
• Functional Keywords: heat-shock, client-binding, holdase, unfolding, chaperone
• Biological source: Leishmania infantum
• Total number of polymer chains: 10
• Total formula weight: 254001.31

Authors

Teixeira, F.,Tse, E.,Makepeace, K.A.T.,Borchers, C.H.,Castro, H.,Tomas, A.M.,Poole, L.B.,Southworth, D.R.,Jakob, U. (deposition date: 2018-07-06, release date: 2019-02-20, Last modification date: 2024-03-13)

Primary citation

Teixeira, F.,Tse, E.,Castro, H.,Makepeace, K.A.T.,Meinen, B.A.,Borchers, C.H.,Poole, L.B.,Bardwell, J.C.,Tomas, A.M.,Southworth, D.R.,Jakob, U.
Chaperone activation and client binding of a 2-cysteine peroxiredoxin.
Nat Commun, 10:659-659, 2019

PubMed Abstract: Many 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.

PubMed: 30737390
DOI: 10.1038/s41467-019-08565-8

Experimental method

ELECTRON MICROSCOPY (3.7 Å)