|Entry||Database: EMDB / ID: EMD-12773|
|Title||Single particle cryo-EM reconstruction of a 40-mer assembly of recombinant yeast Hsp26.|
|Sample||40mer 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 species||Saccharomyces cerevisiae (baker's yeast)|
|Method||single particle reconstruction / cryo EM / Resolution: 9.6 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_12773.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 40mer complex of WT Hsp26
|Entire||Name: 40mer complex of WT Hsp26 / Number of Components: 2|
-Component #1: protein, 40mer complex of WT Hsp26
|Protein||Name: 40mer complex of WT Hsp26 / Recombinant expression: No|
|Mass||Theoretical: 955.2 kDa|
|Source||Species: Saccharomyces cerevisiae (baker's yeast)|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pQE60::HSP26 / Strain: HB101|
-Component #2: protein, Hsp26
|Protein||Name: Hsp26 / Recombinant expression: No|
|Source||Species: Saccharomyces cerevisiae (baker's yeast)|
|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: 29 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: 2463|
-Aug 12, 2020. Covid-19 info
New page: Covid-19 featured information page in EM Navigator.
Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data
-Mar 5, 2020. Novel coronavirus structure data
Novel coronavirus structure data
- International Committee on Taxonomy of Viruses (ICTV) defined the short name of the 2019 coronavirus as "SARS-CoV-2".
- The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2 - nature microbiology
- In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info
+Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
- The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
- The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
+Jul 12, 2017. Major update of PDB
Major update of PDB
- wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
- This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
- In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
- Now, EM Navigator and Yorodumi are based on the updated data.
+Jun 16, 2017. Omokage search with filter
Omokage search with filter
Result of Omokage search can be filtered by keywords and the database types
Related info.:Omokage search
Thousand views of thousand structures
- Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
- This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
- The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi