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- EMDB-52195: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1 -

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Basic information

Entry
Database: EMDB / ID: EMD-52195
TitleHsp70-NBD:Bag1:Rpn1 ternary complex class 1
Map dataDeepemhancer processed map
Sample
  • Complex: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1
KeywordsHsp70 / Chaperone / cochaperone / proteasome / protein degradation
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.8 Å
AuthorsCheng TC / Sakata E / Muntaner J / Maestro-Lopez M / Cuellar J / Valpuesta JM
Funding support Germany, Spain, 6 items
OrganizationGrant numberCountry
German Research Foundation (DFG)154113120 Germany
German Research Foundation (DFG)EXC 2067/1-390729940 Germany
German Research Foundation (DFG)448415290 Germany
Spanish Ministry of Science, Innovation, and UniversitiesPID2022-137175NB-I00 Spain
Spanish Ministry of Science, Innovation, and UniversitiesAEI/10.13039/501100011033 Spain
Spanish Ministry of Science, Innovation, and UniversitiesCEX2023-001386-S Spain
CitationJournal: Sci Adv / Year: 2026
Title: Structures of the 26 proteasome in complex with the Hsp70 co-chaperone Bag1 reveal a mechanism for direct substrate transfer.
Authors: Moisés Maestro-López / Tat Cheung Cheng / Jimena Muntaner / Margarita Menéndez / Melissa Alonso / Andreas Schweitzer / Masato Ishizaka / Robert J Tomko / Jorge Cuéllar / José María ...Authors: Moisés Maestro-López / Tat Cheung Cheng / Jimena Muntaner / Margarita Menéndez / Melissa Alonso / Andreas Schweitzer / Masato Ishizaka / Robert J Tomko / Jorge Cuéllar / José María Valpuesta / Eri Sakata /
Abstract: Coupling between the chaperone and degradation systems, particularly under stress, is essential for eliminating unfolded proteins. The co-chaperone Bag1 links Hsp70 to the 26 proteasome, recruiting ...Coupling between the chaperone and degradation systems, particularly under stress, is essential for eliminating unfolded proteins. The co-chaperone Bag1 links Hsp70 to the 26 proteasome, recruiting Hsp70-bound clients for proteasomal degradation. Here, we present cryo-electron microscopy structures of the Bag1-bound 26 proteasome, revealing unprecedented conformational rearrangements within the 19 regulatory particle. Bag1 binding to the Rpn1 induces a marked reconfiguration of AAA adenosine triphosphatase (ATPase) ring, disrupting its canonical spiral staircase and remodeling the central channel architecture. This reconfiguration generates a large cavity above the substrate entry gate of the 20 core particle. The conserved pore-2 loops of ATPases Rpt2 and Rpt5 play critical roles in opening of the 20 gate, enabling substrate entry into proteolytic chamber independently of ubiquitination. These findings suggest a previously unknown mechanism of the proteasomal degradation, by which remodeling the central cavity and 20 gate in the presence of Bag1, possibly bypassing the need for ubiquitination.
History
DepositionNov 27, 2024-
Header (metadata) releaseDec 31, 2025-
Map releaseDec 31, 2025-
UpdateMar 4, 2026-
Current statusMar 4, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52195.png

Downloads & links

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Map

FileDownload / File: emd_52195.map.gz / Format: CCP4 / Size: 10.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationDeepemhancer processed map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.59 Å/pix.
x 140 pix.
= 222.6 Å		1.59 Å/pix.
x 140 pix.
= 222.6 Å		1.59 Å/pix.
x 140 pix.
= 222.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.59 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.0029895678 - 1.5065764
Average (Standard dev.)0.0013923388 (±0.02858874)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions140140140
Spacing140140140
CellA=B=C: 222.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: B-factor sharpened map

Fileemd_52195_additional_1.map
AnnotationB-factor sharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_52195_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_52195_half_map_2.map
Projections & Slices
AxesZYX

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Density Histograms

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Histogram (log scale)

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Sample components

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Entire : Hsp70-NBD:Bag1:Rpn1 ternary complex class 1

EntireName: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1
Components
  • Complex: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1

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Supramolecule #1: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1

SupramoleculeName: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#33
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.6
Component:
ConcentrationFormulaName
20.0 mMHepesHepes
150.0 mMKClPotassium chloride
1.0 mMDTTDithiothreitol
GridModel: UltrAuFoil R1.2/1.3 / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 42.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.4000000000000001 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 25238
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Details: Cryosparc Ab-initio Reconstruction
Final angle assignmentType: MAXIMUM LIKELIHOOD

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