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- EMDB-0022: Symmetry-free cryo-EM map of TRiC-ADP-BeFx -

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Basic information

Entry
Database: EMDB / ID: EMD-0022
TitleSymmetry-free cryo-EM map of TRiC-ADP-BeFx
Map data
Sample
  • Complex: Bovine TRiC in ADP-BeFx state
Biological speciesBos taurus (cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.6 Å
AuthorsStrauss M / Milicic 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 19, 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_0022.png

Downloads & links

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Map

FileDownload / File: emd_0022.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: 0.0585
Minimum - Maximum-0.11910982 - 0.35609964
Average (Standard dev.)0.0009467982 (±0.01279276)
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 ADP-BeFx state

EntireName: Bovine TRiC in ADP-BeFx state
Components
  • Complex: Bovine TRiC in ADP-BeFx state

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Supramolecule #1: Bovine TRiC in ADP-BeFx state

SupramoleculeName: Bovine TRiC in ADP-BeFx state / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 1 MDa

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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 KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Sampling interval: 5.0 µm / Digitization - Frames/image: 2-47 / Number grids imaged: 1 / Number real images: 7972 / Average exposure time: 12.0 sec. / Average electron dose: 70.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 7.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 151594
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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