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- EMDB-0015: Symmetry-free cryo-EM map of GroEL-actin -

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Basic information

Entry
Database: EMDB / ID: EMD-0015
TitleSymmetry-free cryo-EM map of GroEL-actin
Map data
Sample
  • Complex: GroEL in complex with actin
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 10.3 Å
AuthorsMilicic G / Balchin D / Hayer-Hartl M / Hartl FU
CitationJournal: Cell / Year: 2018
Title: Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC.
Authors: David Balchin / Goran Miličić / Mike Strauss / Manajit Hayer-Hartl / F Ulrich Hartl /
Abstract: The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. Here, ...The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. Here, we use spectroscopic and structural techniques to determine how TRiC promotes the conformational progression of actin to the native state. We find that actin fails to fold spontaneously even in the absence of aggregation but populates a kinetically trapped, conformationally dynamic state. Binding of this frustrated intermediate to TRiC specifies an extended topology of actin with native-like secondary structure. In contrast, GroEL stabilizes bound actin in an unfolded state. ATP binding to TRiC effects an asymmetric conformational change in the chaperonin ring. This step induces the partial release of actin, priming it for folding upon complete release into the chaperonin cavity, mediated by ATP hydrolysis. Our results reveal how the unique features of TRiC direct the folding pathway of an obligate eukaryotic substrate.
History
DepositionMay 18, 2018-
Header (metadata) releaseJun 20, 2018-
Map releaseAug 22, 2018-
UpdateSep 19, 2018-
Current statusSep 19, 2018Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0797
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0797
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0015.png

Downloads & links

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Map

FileDownload / File: emd_0015.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.85 Å
Density
Contour LevelBy AUTHOR: 0.0797 / Movie #1: 0.0797
Minimum - Maximum-0.11295794 - 0.27922672
Average (Standard dev.)0.0012513183 (±0.01309029)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 473.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.851.851.85
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z473.600473.600473.600
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.1130.2790.001

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Supplemental data

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Sample components

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Entire : GroEL in complex with actin

EntireName: GroEL in complex with actin
Components
  • Complex: GroEL in complex with actin

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Supramolecule #1: GroEL in complex with actin

SupramoleculeName: GroEL in complex with actin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
Molecular weightTheoretical: 842 KDa

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 40.0 e/Å2

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Image processing

Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 10.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 10424
FSC plot (resolution estimation)

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