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Yorodumi- EMDB-1914: Structural Dynamics of Archaeal Small Heat Shock Protein Hsp20.2 ... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1914 | |||||||||
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Title | Structural Dynamics of Archaeal Small Heat Shock Protein Hsp20.2 from Archaeoglobus fulgidus | |||||||||
Map data | This is an image of a surface rendered small Hsp20.2 24mer | |||||||||
Sample |
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Keywords | Small heat-shock-protein / protein dynamics / negative stain electron microscopy / three-dimensional reconstruction / chaperone | |||||||||
Biological species | Archaeoglobus fulgidus (archaea) | |||||||||
Method | single particle reconstruction / negative staining / Resolution: 20.0 Å | |||||||||
Authors | Haslbeck M / Kastenmueller A / Buchner J / Weinkauf S / Braun N | |||||||||
Citation | Journal: J Mol Biol / Year: 2008 Title: Structural dynamics of archaeal small heat shock proteins. Authors: Martin Haslbeck / Andreas Kastenmüller / Johannes Buchner / Sevil Weinkauf / Nathalie Braun / Abstract: Small heat shock proteins (sHsps) are a widespread and diverse class of molecular chaperones. In vivo, sHsps contribute to thermotolerance. Recent evidence suggests that their function in the ...Small heat shock proteins (sHsps) are a widespread and diverse class of molecular chaperones. In vivo, sHsps contribute to thermotolerance. Recent evidence suggests that their function in the cellular chaperone network is to maintain protein homeostasis by complexing a variety of non-native proteins. One of the most characteristic features of sHsps is their organization into large, sphere-like structures commonly consisting of 12 or 24 subunits. Here, we investigated the functional and structural properties of Hsp20.2, an sHsp from Archaeoglobus fulgidus, in comparison to its relative, Hsp16.5 from Methanocaldococcus jannaschii. Hsp20.2 is active in suppressing the aggregation of different model substrates at physiological and heat-stress temperatures. Electron microscopy showed that Hsp20.2 forms two distinct types of octahedral oligomers of slightly different sizes, indicating certain structural flexibility of the oligomeric assembly. By three-dimensional analysis of electron microscopic images of negatively stained specimens, we were able to reconstitute 3D models of the assemblies at a resolution of 19 A. Under conditions of heat stress, the distribution of the structurally different Hsp20.2 assemblies changed, and this change was correlated with an increased chaperone activity. In analogy to Hsp20.2, Hsp16.5 oligomers displayed structural dynamics and exhibited increased chaperone activity under conditions of heat stress. Thus, temperature-induced conformational regulation of the activity of sHsps may be a general phenomenon in thermophilic archaea. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1914.map.gz | 13.7 MB | EMDB map data format | |
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Header (meta data) | emd-1914-v30.xml emd-1914.xml | 7 KB 7 KB | Display Display | EMDB header |
Images | EMDB1914.jpg | 99.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1914 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1914 | HTTPS FTP |
-Validation report
Summary document | emd_1914_validation.pdf.gz | 196.1 KB | Display | EMDB validaton report |
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Full document | emd_1914_full_validation.pdf.gz | 195.2 KB | Display | |
Data in XML | emd_1914_validation.xml.gz | 5.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1914 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1914 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_1914.map.gz / Format: CCP4 / Size: 31.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | This is an image of a surface rendered small Hsp20.2 24mer | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.59 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Hsp 20.2 from Archaeoglobus fulgidus, small assembly
Entire | Name: Hsp 20.2 from Archaeoglobus fulgidus, small assembly |
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Components |
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-Supramolecule #1000: Hsp 20.2 from Archaeoglobus fulgidus, small assembly
Supramolecule | Name: Hsp 20.2 from Archaeoglobus fulgidus, small assembly / type: sample / ID: 1000 / Oligomeric state: 24mer, octahedral symmetry / Number unique components: 1 |
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-Macromolecule #1: Heat shock Protein
Macromolecule | Name: Heat shock Protein / type: protein_or_peptide / ID: 1 / Name.synonym: small Hsp / Oligomeric state: 24mer / Recombinant expression: No |
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Source (natural) | Organism: Archaeoglobus fulgidus (archaea) |
-Experimental details
-Structure determination
Method | negative staining |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.44 mg/mL |
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Buffer | pH: 7 / Details: 50 mM Tris, pH 7.0 |
Staining | Type: NEGATIVE / Details: Staining with 1.5% (w/v) ammonium molybdate |
Vitrification | Cryogen name: NONE / Instrument: OTHER |
-Electron microscopy
Microscope | JEOL 100CX |
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Electron beam | Acceleration voltage: 120 kV / Electron source: TUNGSTEN HAIRPIN |
Electron optics | Calibrated magnification: 50000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Specimen holder: Eucentric / Specimen holder model: JEOL |
-Image processing
CTF correction | Details: Phase flipping |
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Final reconstruction | Applied symmetry - Point group: O (octahedral) / Resolution.type: BY AUTHOR / Resolution: 20.0 Å / Resolution method: FSC 0.5 CUT-OFF / Number images used: 1660 |
Final two d classification | Number classes: 10 |