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- EMDB-0018: Symmetry-free cryo-EM map of TRiC-actin-alpha_CCT1 -

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Basic information

Entry
Database: EMDB / ID: EMD-0018
TitleSymmetry-free cryo-EM map of TRiC-actin-alpha_CCT1
Map data
Sample
  • Complex: Bovine TRiC in complex with actin and CCT1 antibody
Biological speciesBos taurus (domestic cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 16.7 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

Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0018.png

Downloads & links

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Map

FileDownload / File: emd_0018.map.gz / Format: CCP4 / Size: 75.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.85 Å/pix.
x 270 pix.
= 499.5 Å		1.85 Å/pix.
x 270 pix.
= 499.5 Å		1.85 Å/pix.
x 270 pix.
= 499.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.85 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0043
Minimum - Maximum-0.026710883 - 0.08491805
Average (Standard dev.)0.0000924297 (±0.0057740486)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions270270270
Spacing270270270
CellA=B=C: 499.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Bovine TRiC in complex with actin and CCT1 antibody

EntireName: Bovine TRiC in complex with actin and CCT1 antibody
Components
  • Complex: Bovine TRiC in complex with actin and CCT1 antibody

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Supramolecule #1: Bovine TRiC in complex with actin and CCT1 antibody

SupramoleculeName: Bovine TRiC in complex with actin and CCT1 antibody / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Bos taurus (domestic cattle)

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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
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 18.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

1960

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 16.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 9685
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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