6MRC

ADP-bound human mitochondrial Hsp60-Hsp10 football complex

Summary for 6MRC

• Entry DOI: 10.2210/pdb6mrc/pdb
• EMDB information: 9195 9196
• Descriptor: 60 kDa heat shock protein, mitochondrial, 10 kDa heat shock protein, mitochondrial, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: complex, adp, football, chaperone
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 28
• Total formula weight: 944432.51

Authors

Gomez-Llorente, Y.,Jebara, F.,Patra, M.,Malik, R.,Nissemblat, S.,Azem, A.,Hirsch, J.A.,Ubarretxena-Belandia, I. (deposition date: 2018-10-12, release date: 2020-04-15, Last modification date: 2025-05-14)

Primary citation

Gomez-Llorente, Y.,Jebara, F.,Patra, M.,Malik, R.,Nisemblat, S.,Chomsky-Hecht, O.,Parnas, A.,Azem, A.,Hirsch, J.A.,Ubarretxena-Belandia, I.
Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.
Nat Commun, 11:1916-1916, 2020

PubMed Abstract: mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES. Here we report the crystal structure of an ATP (ADP:BeF-bound) ground-state mimic double-ring mHsp60-(mHsp10) football complex, and the cryo-EM structures of the ADP-bound successor mHsp60-(mHsp10) complex, and a single-ring mHsp60-mHsp10 half-football. The structures explain the nucleotide dependence of mHsp60 ring formation, and reveal an inter-ring nucleotide symmetry consistent with the absence of negative cooperativity. In the ground-state a two-fold symmetric H-bond and a salt bridge stitch the double-rings together, whereas only the H-bond remains as the equatorial gap increases in an ADP football poised to split into half-footballs. Refolding assays demonstrate obligate single- and double-ring mHsp60 variants are active, and complementation analysis in bacteria shows the single-ring variant is as efficient as wild-type mHsp60. Our work provides a structural basis for active single- and double-ring complexes coexisting in the mHsp60-mHsp10 chaperonin reaction cycle.

PubMed: 32317635
DOI: 10.1038/s41467-020-15698-8

Experimental method

ELECTRON MICROSCOPY (3.08 Å)