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- EMDB-1221: Multiple distinct assemblies reveal conformational flexibility in... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1221 | |||||||||
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Title | Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. | |||||||||
![]() | View down the 2-fold axis of the expanded form of yeast Hsp26 | |||||||||
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Function / homology | ![]() response to salt stress / response to hydrogen peroxide / protein homooligomerization / unfolded protein binding / protein folding / protein complex oligomerization / response to heat / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 10.8 Å | |||||||||
![]() | White HE / Orlova EV / Chen S / Wang L / Ignatiou A / Gowen B / Stromer T / Franzmann TM / Haslbeck M / Buchner J / Saibil HR | |||||||||
![]() | ![]() Title: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Authors: Helen E White / Elena V Orlova / Shaoxia Chen / Luchun Wang / Athanasios Ignatiou / Brent Gowen / Thusnelda Stromer / Titus M Franzmann / Martin Haslbeck / Johannes Buchner / Helen R Saibil / ![]() Abstract: Small heat shock proteins are a superfamily of molecular chaperones that suppress protein aggregation and provide protection from cell stress. A key issue for understanding their action is to define ...Small heat shock proteins are a superfamily of molecular chaperones that suppress protein aggregation and provide protection from cell stress. A key issue for understanding their action is to define the interactions of subunit domains in these oligomeric assemblies. Cryo-electron microscopy of yeast Hsp26 reveals two distinct forms, each comprising 24 subunits arranged in a porous shell with tetrahedral symmetry. The subunits form elongated, asymmetric dimers that assemble via trimeric contacts. Modifications of both termini cause rearrangements that yield a further four assemblies. Each subunit contains an N-terminal region, a globular middle domain, the alpha-crystallin domain, and a C-terminal tail. Twelve of the C termini form 3-fold assembly contacts which are inserted into the interior of the shell, while the other 12 C termini form contacts on the surface. Hinge points between the domains allow a variety of assembly contacts, providing the flexibility required for formation of supercomplexes with non-native proteins. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.2 KB 9.2 KB | Display Display | ![]() |
Images | ![]() | 54.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2h50MC ![]() 1226C ![]() 1227C ![]() 1228C ![]() 1229C ![]() 1230C ![]() 2h53C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | View down the 2-fold axis of the expanded form of yeast Hsp26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.86 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : yeast small heat shock protein 26
Entire | Name: yeast small heat shock protein 26 |
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Components |
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-Supramolecule #1000: yeast small heat shock protein 26
Supramolecule | Name: yeast small heat shock protein 26 / type: sample / ID: 1000 / Oligomeric state: 24-mer / Number unique components: 1 |
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-Macromolecule #1: Hsp26
Macromolecule | Name: Hsp26 / type: protein_or_peptide / ID: 1 / Oligomeric state: 24-mer / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.0 mg/mL |
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Buffer | pH: 7.4 / Details: 40 mM Hepes, 50 mM NaCl, 2 mM EDTA, 1 mM DTT |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI/PHILIPS CM200FEG |
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Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 1.86 µm / Number real images: 21 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 36080 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.4 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 38000 |
Sample stage | Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN |
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Image processing
CTF correction | Details: Phase flipping |
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Final reconstruction | Applied symmetry - Point group: T (tetrahedral) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 10.8 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: Imagic / Details: Angular reconstitution / Number images used: 10000 |
Final two d classification | Number classes: 1300 |
-Atomic model buiding 1
Initial model | PDB ID: |
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Software | Name: URO |
Details | Protocol: Rigid Body. The alpha-crystallin domains were fitted in the program O, prior to refinement. |
Refinement | Space: RECIPROCAL / Protocol: RIGID BODY FIT |
Output model | ![]() PDB-2h50: |