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- PDB-13kw: Human Single-ring Hsp10 -

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Basic information

Entry
Database: PDB / ID: 13kw
TitleHuman Single-ring Hsp10
Components10 kDa heat shock protein, mitochondrial
KeywordsCHAPERONE / Hsp10 / Hsp60 / cochaperone / cryo-EM
Function / homology
Function and homology information


RHOG GTPase cycle / response to unfolded protein / Mitochondrial unfolded protein response (UPRmt) / protein folding chaperone / intrinsic apoptotic signaling pathway / osteoblast differentiation / : / protein-folding chaperone binding / protein folding / mitochondrial matrix ...RHOG GTPase cycle / response to unfolded protein / Mitochondrial unfolded protein response (UPRmt) / protein folding chaperone / intrinsic apoptotic signaling pathway / osteoblast differentiation / : / protein-folding chaperone binding / protein folding / mitochondrial matrix / mitochondrion / RNA binding / extracellular exosome / ATP binding / membrane / metal ion binding
Similarity search - Function
Chaperonin GroES, conserved site / Chaperonins cpn10 signature. / Chaperonin 10 Kd subunit / GroES chaperonin family / GroES chaperonin superfamily / Chaperonin 10 Kd subunit / GroES-like superfamily
Similarity search - Domain/homology
10 kDa heat shock protein, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å
AuthorsPage, A.A. / Walti, M.A.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R00GM132496 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM156786 United States
CitationJournal: bioRxiv / Year: 2026
Title: Hsp10: From Single to Double Rings-Structural Basis of Protein Homeostasis.
Authors: Abigail Page / Wyatt Hendricks / Aranea Dunckley / Marielle A Wälti
Abstract: The human chaperone complex Hsp60/Hsp10 is essential for maintaining cellular proteostasis by preventing protein misfolding and aggregation. Disruption of these processes contributes to ...The human chaperone complex Hsp60/Hsp10 is essential for maintaining cellular proteostasis by preventing protein misfolding and aggregation. Disruption of these processes contributes to neurodegenerative diseases, while overexpression of Hsp60 and Hsp10 is associated with various cancers. Understanding their molecular mechanisms is therefore of fundamental importance. Unlike its bacterial homolog GroEL, human Hsp60 adopts multiple oligomeric states, with both heptameric and tetradecameric forms binding Hsp10 to form a folding cavity for substrate refolding. Here, we determine the cryo-EM structure of apo Hsp10 and find that, in addition to its single-ring form, it also assembles into a compact double-ring state. This reveals that Hsp10, like Hsp60, exhibits structural behavior that differs markedly from its bacterial counterpart. Traditionally viewed as a passive cofactor assisting Hsp60, we show that Hsp10 alone possesses intrinsic chaperone activity: it supports folding of natural substrates such as malate dehydrogenase 1 and manganese superoxide dismutase. NMR analysis further shows that substrate binding occurs primarily at the core of Hsp10 rather than at the loops. Our findings suggest that Hsp10 exists in equilibrium between single- and double-ring complexes in the unbound state, and upon binding as a single-ring complex, it actively guides substrates into the folding chamber.
History
DepositionMay 12, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 15, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 15, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 10 kDa heat shock protein, mitochondrial
B: 10 kDa heat shock protein, mitochondrial
C: 10 kDa heat shock protein, mitochondrial
D: 10 kDa heat shock protein, mitochondrial
E: 10 kDa heat shock protein, mitochondrial
F: 10 kDa heat shock protein, mitochondrial
G: 10 kDa heat shock protein, mitochondrial


Theoretical massNumber of molelcules
Total (without water)76,6277
Polymers76,6277
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
10 kDa heat shock protein, mitochondrial / Hsp10 / 10 kDa chaperonin / Chaperonin 10 / CPN10 / Early-pregnancy factor / EPF / Heat shock ...Hsp10 / 10 kDa chaperonin / Chaperonin 10 / CPN10 / Early-pregnancy factor / EPF / Heat shock protein family E member 1


Mass: 10946.674 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HSPE1 / Production host: Escherichia coli (E. coli) / References: UniProt: P61604
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Single-Ring Human Hsp10 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 76 kDa/nm / Experimental value: YES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.4
Buffer component
IDConc.NameFormulaBuffer-ID
1300 mMsodium chlorideNaCl1
210 mMmagnesium chlorideMgCl21
320 mMpotassium chlorideKCl1
420 mMmagnesium acetateMg(CH3COO)21
550 mMtris1
SpecimenConc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 80 % / Chamber temperature: 283 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER
Electron lensMode: OTHER / Nominal defocus max: 5000 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 BASE (4k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING ONLY
3D reconstructionResolution: 4 Å / Resolution method: OTHER / Num. of particles: 46178 / Symmetry type: POINT

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