|Entry||Database: EMDB / ID: EMD-12766|
|Title||Single particle cryo-EM reconstruction of just the top two rings of a 40-mer assembly of recombinant yeast Hsp26 S207E mutant.|
|Sample||Top two rings (16 subunits) of a 40mer complex of Hsp26 mutant S207E. (use 0.487 as threshold to visualise)|
|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 species||Saccharomyces cerevisiae (baker's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)|
|Method||single particle reconstruction / cryo EM / Resolution: 7.8 Å|
|Authors||Muehlhofer M / Peters C / Kriehuber T / Kreuzeder M / Kazman P / Rodina N / Reif B / Haslbeck M / Weinkauf S / Buchner J|
|Funding support|| Germany, 1 items |
|Citation||Journal: 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.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_12766.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.33 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Top two rings (16 subunits) of a 40mer complex of Hsp26 mutant S2...
|Entire||Name: Top two rings (16 subunits) of a 40mer complex of Hsp26 mutant S207E. (use 0.487 as threshold to visualise)|
Number of Components: 2
-Component #1: protein, Top two rings (16 subunits) of a 40mer complex of Hsp26 ...
|Protein||Name: Top two rings (16 subunits) of a 40mer complex of Hsp26 mutant S207E. (use 0.487 as threshold to visualise)|
Recombinant expression: No
|Mass||Theoretical: 382 kDa|
|Source||Species: Saccharomyces cerevisiae (baker's yeast)|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pQE60::HSP26 / Strain: HB101|
-Component #2: protein, Heat shock protein 26
|Protein||Name: Heat shock protein 26Heat shock response / Number of Copies: 5 / Recombinant expression: No|
|Mass||Theoretical: 23.910586 kDa|
|Source||Species: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)|
Strain: ATCC 204508 / S288c
|Source (engineered)||Expression System: Escherichia coli HB101 (bacteria)|
|Specimen||Specimen State: Particle / Method: cryo EM|
|Sample solution||pH: 7.4|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen Name: OTHER / Temperature: 294 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron Source: FIELD EMISSION GUN / Accelerating Voltage: 300 kV / Electron Dose: 45 e/Å2 / Illumination Mode: FLOOD BEAM|
|Lens||Magnification: 105000.0 X (nominal) / Cs: 2.7 mm / Imaging Mode: BRIGHT FIELD / Defocus: 600.0 - 2800.0 nm / Energy Filter: GIF Quantum LS|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of Digital Images: 5010|
-Atomic model buiding
|Modeling #1||Refinement protocol: flexible / Target Criteria: Correlation coefficient / Refinement space: REAL|
Details: Homology model generated with ITASSER with 1GME as template. Fitted with Chimera and flexibly fitted with NAMD. Residues 63 to 214 present in the model.
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