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- EMDB-4294: Hsp90:p53-TMGST:CHIP -

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Basic information

Entry
Database: EMDB / ID: EMD-4294
TitleHsp90:p53-TMGST:CHIP
Map dataHsp90:p53-TMGST:CHIP
Sample
  • Complex: Hsp90:p53-TMGST:CHIP
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 13.0 Å
AuthorsQuintana-Gallardo L / Martin-Benito J / Valpuesta JM
CitationJournal: Sci Rep / Year: 2019
Title: The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism.
Authors: Lucía Quintana-Gallardo / Jaime Martín-Benito / Miguel Marcilla / Guadalupe Espadas / Eduard Sabidó / José María Valpuesta /
Abstract: Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case for Hsp70 and Hsp90 which, in ...Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case for Hsp70 and Hsp90 which, in concert with the cochaperone CHIP, direct their bound substrate to degradation through ubiquitination. We generated complexes between the chaperones (Hsp70 or Hsp90), the cochaperone CHIP and, as substrate, a p53 variant containing the GST protein (p53-TMGST). Both ternary complexes (Hsp70:p53-TMGST:CHIP and Hsp90:p53-TMGST:CHIP) ubiquitinated the substrate at a higher efficiency than in the absence of the chaperones. The 3D structures of the two complexes, obtained using a combination of cryoelectron microscopy and crosslinking mass spectrometry, showed the substrate located between the chaperone and the cochaperone, suggesting a ubiquitination mechanism in which the chaperone-bound substrate is presented to CHIP. These complexes are inherently flexible, which is important for the ubiquitination process.
History
DepositionFeb 7, 2018-
Header (metadata) releaseMar 14, 2018-
Map releaseMar 20, 2019-
UpdateOct 2, 2019-
Current statusOct 2, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0144
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.0144
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4294.png

Downloads & links

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Map

FileDownload / File: emd_4294.map.gz / Format: CCP4 / Size: 1.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationHsp90:p53-TMGST:CHIP
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
4.11 Å/pix.
x 76 pix.
= 312.36 Å		4.11 Å/pix.
x 76 pix.
= 312.36 Å		4.11 Å/pix.
x 76 pix.
= 312.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 4.11 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0144 / Movie #1: 0.0144
Minimum - Maximum-0.03796128 - 0.3141349
Average (Standard dev.)-0.0009451509 (±0.017232796)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions767676
Spacing767676
CellA=B=C: 312.36002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.114.114.11
M x/y/z767676
origin x/y/z0.0000.0000.000
length x/y/z312.360312.360312.360
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ320320320
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS767676
D min/max/mean-0.0380.314-0.001

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Supplemental data

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Sample components

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Entire : Hsp90:p53-TMGST:CHIP

EntireName: Hsp90:p53-TMGST:CHIP
Components
  • Complex: Hsp90:p53-TMGST:CHIP

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Supramolecule #1: Hsp90:p53-TMGST:CHIP

SupramoleculeName: Hsp90:p53-TMGST:CHIP / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
Molecular weightTheoretical: 200 kDa/nm

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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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 30.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 13.0 Å / Resolution method: FSC 0.33 CUT-OFF / Number images used: 10000
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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