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- EMDB-1889: Structural Dynamics of Archaeal Small Heat Shock Protein Hsp20.2 ... -

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Basic information

Entry
Database: EMDB / ID: EMD-1889
TitleStructural Dynamics of Archaeal Small Heat Shock Protein Hsp20.2 from Archaeoglobus fulgidus
Map dataLarge Hsp20.2 assembly
Sample
  • Sample: Hsp 20.2 from Archaeoglobus fulgidus
  • Protein or peptide: Heat shock Protein
Keywordssmall heat-shock-protein / protein dynamics / three-dimensional reconstruction / chaperone
Biological speciesArchaeoglobus fulgidus (archaea)
Methodsingle particle reconstruction / negative staining / Resolution: 19.0 Å
AuthorsHaslbeck M / Kastenmueller A / Buchner J / Weinkauf S / Braun N
CitationJournal: 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
DepositionApr 5, 2011-
Header (metadata) releaseJul 8, 2011-
Map releaseJul 8, 2011-
UpdateJul 8, 2011-
Current statusJul 8, 2011Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

EMDB1889.jpg

Downloads & links

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Map

FileDownload / File: emd_1889.map.gz / Format: CCP4 / Size: 31.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLarge Hsp20.2 assembly
Voxel size
XYZ
EMDB info.111
CCP4 map header111
EM Navigator Movie #11.591.591.59
Density
Contour LevelBy AUTHOR: 0.011 / Movie #1: 0.011
Minimum - Maximum-0.0266003 - 0.0381285
Average (Standard dev.)0.0000348784 (±0.00562553)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-102-102-102
Dimensions204204204
Spacing204204204
CellA=B=C: 204 Å
α=β=γ: 90 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z111
M x/y/z204204204
origin x/y/z-0.000-0.000-0.000
length x/y/z204.000204.000204.000
α/β/γ90.00090.00090.000
start NX/NY/NZ-56-56-55
NX/NY/NZ112112112
MAP C/R/S123
start NC/NR/NS-102-102-102
NC/NR/NS204204204
D min/max/mean-0.0270.0380.000

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Supplemental data

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Sample components

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Entire : Hsp 20.2 from Archaeoglobus fulgidus

EntireName: Hsp 20.2 from Archaeoglobus fulgidus
Components
  • Sample: Hsp 20.2 from Archaeoglobus fulgidus
  • Protein or peptide: Heat shock Protein

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Supramolecule #1000: Hsp 20.2 from Archaeoglobus fulgidus

SupramoleculeName: Hsp 20.2 from Archaeoglobus fulgidus / type: sample / ID: 1000 / Oligomeric state: 24mer, octahedral symmetry / Number unique components: 1

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Macromolecule #1: Heat shock Protein

MacromoleculeName: Heat shock Protein / type: protein_or_peptide / ID: 1 / Name.synonym: Small Hsp / Oligomeric state: 24mer / Recombinant expression: No
Source (natural)Organism: Archaeoglobus fulgidus (archaea)

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Experimental details

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Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.44 mg/mL
BufferpH: 7 / Details: 50 mM Tris, pH 7.0
StainingType: NEGATIVE / Details: Staining with 1.5% (w/v) ammonium molybdate
VitrificationCryogen name: NONE / Instrument: OTHER

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Electron microscopy

MicroscopeJEOL 2010
Electron beamAcceleration voltage: 120 kV / Electron source: LAB6
Electron opticsCalibrated magnification: 50000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Sample stageSpecimen holder: Eucentric / Specimen holder model: JEOL

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Image processing

CTF correctionDetails: Phase flipping
Final reconstructionApplied symmetry - Point group: O (octahedral) / Resolution.type: BY AUTHOR / Resolution: 19.0 Å / Resolution method: FSC 0.5 CUT-OFF / Number images used: 4484
Final two d classificationNumber classes: 10

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