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- EMDB-12773: Single particle cryo-EM reconstruction of a 40-mer assembly of re... -

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Basic information

Database: EMDB / ID: EMD-12773
TitleSingle particle cryo-EM reconstruction of a 40-mer assembly of recombinant yeast Hsp26.
Map data
Sample40mer complex of WT Hsp26:
Function / homology
Function and homology information

cytoplasmic stress granule / unfolded protein binding / cellular response to heat / protein folding / mRNA binding / mitochondrion / identical protein binding / nucleus / cytoplasm
Similarity search - Function
: / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone
Similarity search - Domain/homology
Heat shock protein 26
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (baker's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 9.6 Å
AuthorsMuehlhofer M / Peters C / Kriehuber T / Kreuzeder M / Kazman P / Rodina N / Reif B / Haslbeck M / Weinkauf S / Buchner J
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG)SFB 1035 Germany
CitationJournal: Nat Commun / Year: 2021
Title: Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
Authors: Moritz Mühlhofer / Carsten Peters / Thomas Kriehuber / Marina Kreuzeder / Pamina Kazman / Natalia Rodina / Bernd Reif / Martin Haslbeck / Sevil Weinkauf / Johannes Buchner /
Abstract: Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. Its chaperone activity is activated by oligomer dissociation at heat shock temperatures. Hsp26 contains 9 phosphorylation sites in ...Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. Its chaperone activity is activated by oligomer dissociation at heat shock temperatures. Hsp26 contains 9 phosphorylation sites in different structural elements. Our analysis of phospho-mimetic mutations shows that phosphorylation activates Hsp26 at permissive temperatures. The cryo-EM structure of the Hsp26 40mer revealed contacts between the conserved core domain of Hsp26 and the so-called thermosensor domain in the N-terminal part of the protein, which are targeted by phosphorylation. Furthermore, several phosphorylation sites in the C-terminal extension, which link subunits within the oligomer, are sensitive to the introduction of negative charges. In all cases, the intrinsic inhibition of chaperone activity is relieved and the N-terminal domain becomes accessible for substrate protein binding. The weakening of domain interactions within and between subunits by phosphorylation to activate the chaperone activity in response to proteotoxic stresses independent of heat stress could be a general regulation principle of sHsps.
DepositionApr 19, 2021-
Header (metadata) releaseNov 24, 2021-
Map releaseNov 24, 2021-
UpdateDec 1, 2021-
Current statusDec 1, 2021Processing site: PDBe / Status: Released

Structure visualization

  • Surface view with section colored by density value
  • Surface level: 0.397
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.397
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
Supplemental images

Downloads & links


FileDownload / File: emd_12773.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

AxesZ (Sec.)Y (Row.)X (Col.)
1.33 Å/pix.
x 288 pix.
= 383.04 Å
1.33 Å/pix.
x 288 pix.
= 383.04 Å
1.33 Å/pix.
x 288 pix.
= 383.04 Å



Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.33 Å
Contour LevelBy AUTHOR: 0.397 / Movie #1: 0.397
Minimum - Maximum-0.15164986 - 1.0715672
Average (Standard dev.)0.009759683 (±0.07844891)
SymmetrySpace group: 1


Map geometry
Axis orderXYZ
CellA=B=C: 383.04 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.331.331.33
M x/y/z288288288
origin x/y/z0.0000.0000.000
length x/y/z383.040383.040383.040
start NX/NY/NZ000
MAP C/R/S123
start NC/NR/NS000
D min/max/mean-0.1521.0720.010

Supplemental data

Sample components

Entire 40mer complex of WT Hsp26

EntireName: 40mer complex of WT Hsp26 / Number of Components: 2

Component #1: protein, 40mer complex of WT Hsp26

ProteinName: 40mer complex of WT Hsp26 / Recombinant expression: No
MassTheoretical: 955.2 kDa
SourceSpecies: Saccharomyces cerevisiae (baker's yeast)
Source (engineered)Expression System: Escherichia coli (E. coli) / Vector: pQE60::HSP26 / Strain: HB101

Component #2: protein, Hsp26

ProteinName: Hsp26 / Recombinant expression: No
SourceSpecies: Saccharomyces cerevisiae (baker's yeast)
Source (engineered)Expression System: Escherichia coli HB101 (bacteria)

Experimental details

Sample preparation

SpecimenSpecimen State: Particle / Method: cryo EM
Sample solutionpH: 7.4
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen Name: OTHER / Temperature: 294 K / Humidity: 100 %

Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron Source: FIELD EMISSION GUN / Accelerating Voltage: 300 kV / Electron Dose: 29 e/Å2 / Illumination Mode: FLOOD BEAM
LensMagnification: 105000.0 X (nominal) / Cs: 2.7 mm / Imaging Mode: BRIGHT FIELD / Defocus: 600.0 - 2800.0 nm / Energy Filter: GIF Quantum LS
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

Image acquisition

Image acquisitionNumber of Digital Images: 2463

Image processing

ProcessingMethod: single particle reconstruction / Applied Symmetry: C4 (4 fold cyclic) / Number of Projections: 85425
3D reconstructionSoftware: cryoSPARC / Resolution: 9.6 Å / Resolution Method: FSC 0.143 CUT-OFF
FSC plot (resolution estimation)

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