7YWY

Structure of the GroEL chaperonin in complex with the CnoX chaperedoxin

Summary for 7YWY

• Entry DOI: 10.2210/pdb7ywy/pdb
• EMDB information: 14352
• Descriptor: Chaperedoxin, Chaperonin GroEL (2 entities in total)
• Functional Keywords: protein folding, redox, complex, chaperonin, chaperone
• Biological source: Escherichia coli; More
• Total number of polymer chains: 28
• Total formula weight: 909888.39

Authors

Van der Verren, S.E.,Remaut, H.,Collet, J.F.,Dupuy, E. (deposition date: 2022-02-15, release date: 2023-02-22, Last modification date: 2024-09-04)

Primary citation

Dupuy, E.,Van der Verren, S.E.,Lin, J.,Wilson, M.A.,Dachsbeck, A.V.,Viela, F.,Latour, E.,Gennaris, A.,Vertommen, D.,Dufrene, Y.F.,Iorga, B.I.,Goemans, C.V.,Remaut, H.,Collet, J.F.
A molecular device for the redox quality control of GroEL/ES substrates.
Cell, 186:1039-1049.e17, 2023

PubMed Abstract: Hsp60 chaperonins and their Hsp10 cofactors assist protein folding in all living cells, constituting the paradigmatic example of molecular chaperones. Despite extensive investigations of their structure and mechanism, crucial questions regarding how these chaperonins promote folding remain unsolved. Here, we report that the bacterial Hsp60 chaperonin GroEL forms a stable, functionally relevant complex with the chaperedoxin CnoX, a protein combining a chaperone and a redox function. Binding of GroES (Hsp10 cofactor) to GroEL induces CnoX release. Cryoelectron microscopy provided crucial structural information on the GroEL-CnoX complex, showing that CnoX binds GroEL outside the substrate-binding site via a highly conserved C-terminal α-helix. Furthermore, we identified complexes in which CnoX, bound to GroEL, forms mixed disulfides with GroEL substrates, indicating that CnoX likely functions as a redox quality-control plugin for GroEL. Proteins sharing structural features with CnoX exist in eukaryotes, suggesting that Hsp60 molecular plugins have been conserved through evolution.

PubMed: 36764293
DOI: 10.1016/j.cell.2023.01.013

Experimental method

ELECTRON MICROSCOPY (3.4 Å)