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Structure paper

TitleStructural basis for ATP-driven double-ring assembly of the human mitochondrial Hsp60 chaperonin.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateOct 5, 2025
AuthorsIgor Tascón / Jorge P López-Alonso / Yoel Shkolnisky / David Gil-Cartón / Jesús Vilchez-Garcia / Alberto G Berruezo / Yacob Gómez-Llorente / Radhika Malik / Fady Jebara / Malay Patra / Joel A Hirsch / Abdussalam Azem / Iban Ubarretxena-Belandia
PubMed AbstractThe ATP-driven mHsp60:mHsp10 chaperonin system assists protein folding within the mitochondrial matrix of human cells. Substrate protein folding has been proposed to occur through interconnected ...The ATP-driven mHsp60:mHsp10 chaperonin system assists protein folding within the mitochondrial matrix of human cells. Substrate protein folding has been proposed to occur through interconnected single- and double-ring pathways. In the absence of nucleotide, mHsp60 exists in equilibrium between free protomers and heptameric single rings, while the formation of double rings requires ATP. Here, we present cryo-electron microscopy structures of mHsp60 in the apo state, bound to ATP, and bound to ATP in complex with the cochaperonin mHsp10. ATP binding to single-ring apo mHsp60 triggers coordinated conformational changes in the intermediate and apical domains, resulting in a highly dynamic apical region within the ring. Extensive inter-subunit rearrangements flatten the equatorial surface of each ring, thereby enabling inter-ring contacts that stitch the rings together to form double-ring mHsp60 . Collectively, these structures define the structural basis of ATP-driven double-ring assembly of a human mitochondrial chaperonin responsible for maintaining mitochondrial protein homeostasis.
External linksbioRxiv / PubMed:41256524 / PubMed Central
MethodsEM (single particle)
Resolution2.44 - 3.96 Å
Structure data

19930

9es0

EMDB-19930, PDB-9es0:
ATP-bound human mitochondrial Hsp60-Hsp10 football complex
Method: EM (single particle) / Resolution: 2.58 Å

19931

9es1

EMDB-19931, PDB-9es1:
ATP-bound human mitochondrial Hsp60-Hsp10 half football complex
Method: EM (single particle) / Resolution: 2.95 Å

19932

9es2

EMDB-19932, PDB-9es2:
ATP-bound human mitochondrial Hsp60 double-ring complex
Method: EM (single particle) / Resolution: 2.44 Å

19933

9es3

EMDB-19933, PDB-9es3:
Apo human mitochondrial Hsp60
Method: EM (single particle) / Resolution: 3.28 Å

19934

9es4

EMDB-19934, PDB-9es4:
ADP:BeF3-bound human mitochondrial Hsp60-Hsp10 football complex
Method: EM (single particle) / Resolution: 2.91 Å

19935

9es5

EMDB-19935, PDB-9es5:
ADP:BeF3-bound human mitochondrial Hsp60-Hsp10 half-football complex
Method: EM (single particle) / Resolution: 3.5 Å

19936

9es6

EMDB-19936, PDB-9es6:
ADP:BeF3-bound human mitochondrial Hsp60 double-ring complex
Method: EM (single particle) / Resolution: 3.0 Å

51890

9h5s

EMDB-51890, PDB-9h5s:
ATP-bound human mitochondrial Hsp60-Hsp10 football complex (C1)
Method: EM (single particle) / Resolution: 2.98 Å

51891

9h5t

EMDB-51891, PDB-9h5t:
ATP-bound human mitochondrial Hsp60-Hsp10 half football complex (C1)
Method: EM (single particle) / Resolution: 3.44 Å

51892

9h5u

EMDB-51892, PDB-9h5u:
ATP-bound human mitochondrial Hsp60 double-ring complex (C1)
Method: EM (single particle) / Resolution: 3.14 Å

51893

9h5v

EMDB-51893, PDB-9h5v:
Apo human mitochondrial Hsp60 (C1)
Method: EM (single particle) / Resolution: 3.96 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

Source
  • homo sapiens (human)
KeywordsCHAPERONE / mitochondrial / D7-symmetry / C7-symmetry

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