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- EMDB-65492: In situ structure of mtHsp60-Hsp10 bullet-like conformation -

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Basic information

Entry
Database: EMDB / ID: EMD-65492
TitleIn situ structure of mtHsp60-Hsp10 bullet-like conformation
Map data
Sample
  • Cell: Human mitochondrial mtHsp60-Hsp10 chaperone complex
Keywordsmthsp60-hsp10 / CHAPERONE
Biological speciesHomo sapiens (human)
Methodsubtomogram averaging / cryo EM / Resolution: 21.0 Å
AuthorsJung M / Roh S
Funding support Korea, Republic Of, 5 items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea)2019R1C1C1004598 Korea, Republic Of
National Research Foundation (NRF, Korea)2020R1A5A1018081 Korea, Republic Of
National Research Foundation (NRF, Korea)2021M3A9I4021220 Korea, Republic Of
National Research Foundation (NRF, Korea)2019M3E5D6063871 Korea, Republic Of
National Research Foundation (NRF, Korea)2020R1A6C101A183 Korea, Republic Of
CitationJournal: Sci Adv / Year: 2025
Title: In situ characterization of mitochondrial Hsp60-Hsp10 chaperone complex under folding stress.
Authors: Mingyu Jung / Minjung Kim / Su Jin Ham / Jongkyeong Chung / Soung-Hun Roh /
Abstract: Mitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein- ...Mitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein-folding stress. However, how these chaperones mitigate protein-folding stress remains unclear. Here, using correlated cryo-electron tomography, we show that folding stress triggers marked mitochondrial morphological changes, including the accumulation of amorphous protein aggregates and increased abundance and spatial clustering of the mitochondrial heat shock protein 60-heat shock protein 10 (mtHsp60-Hsp10) complex. Subtomogram analysis revealed the in situ architecture and conformational heterogeneity of mtHsp60-Hsp10 under stress, which retains its canonical double-ring structure while adopting distinct football, half-football, and bullet-like states. Notably, the mtHsp60-Hsp10 complex encapsulates unstructured substrates through conserved hydrophobic interactions. We further demonstrate that knockdown of the mtHsp60-Hsp10 complex exacerbates folding stress, as evidenced by elevated cellular stress responses and activation of mitophagy. Our study defines the in situ structural properties of the mtHsp60-Hsp10 complex and provides mechanistic insight into how it safeguards mitochondrial proteostasis under folding stress.
History
DepositionJul 24, 2025-
Header (metadata) releaseOct 1, 2025-
Map releaseOct 1, 2025-
UpdateNov 19, 2025-
Current statusNov 19, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_65492.png

Downloads & links

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Map

FileDownload / File: emd_65492.map.gz / Format: CCP4 / Size: 2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
4.93 Å/pix.
x 80 pix.
= 394.4 Å		4.93 Å/pix.
x 80 pix.
= 394.4 Å		4.93 Å/pix.
x 80 pix.
= 394.4 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 4.93 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.495
Minimum - Maximum-0.2645673 - 1.1922309
Average (Standard dev.)0.030504938 (±0.14472587)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions808080
Spacing808080
CellA=B=C: 394.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_65492_msk_1.map
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Half map: #1

Fileemd_65492_half_map_1.map
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Half map: #2

Fileemd_65492_half_map_2.map
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Sample components

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Entire : Human mitochondrial mtHsp60-Hsp10 chaperone complex

EntireName: Human mitochondrial mtHsp60-Hsp10 chaperone complex
Components
  • Cell: Human mitochondrial mtHsp60-Hsp10 chaperone complex

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Supramolecule #1: Human mitochondrial mtHsp60-Hsp10 chaperone complex

SupramoleculeName: Human mitochondrial mtHsp60-Hsp10 chaperone complex / type: cell / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation statecell

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Sample preparation

BufferpH: 7
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 3.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 3.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

DetailsFalcon4i
Final reconstructionApplied symmetry - Point group: C7 (7 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 21.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number subtomograms used: 592
ExtractionNumber tomograms: 451 / Number images used: 135300 / Software - Name: Warp
CTF correctionType: NONE
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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