+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0018 | |||||||||
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Title | Symmetry-free cryo-EM map of TRiC-actin-alpha_CCT1 | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Bos taurus (cattle) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 16.7 Å | |||||||||
Authors | Milicic G / Balchin D / Hayer-Hartl M / Hartl FU | |||||||||
Citation | Journal: 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 |
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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_0018.map.gz | 58.2 MB | EMDB map data format | |
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Header (meta data) | emd-0018-v30.xml emd-0018.xml | 7.1 KB 7.1 KB | Display Display | EMDB header |
Images | emd_0018.png | 18.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0018 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0018 | HTTPS FTP |
-Validation report
Summary document | emd_0018_validation.pdf.gz | 208.5 KB | Display | EMDB validaton report |
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Full document | emd_0018_full_validation.pdf.gz | 207.6 KB | Display | |
Data in XML | emd_0018_validation.xml.gz | 6.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0018 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0018 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_0018.map.gz / Format: CCP4 / Size: 75.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.85 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 : Bovine TRiC in complex with actin and CCT1 antibody
Entire | Name: Bovine TRiC in complex with actin and CCT1 antibody |
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Components |
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-Supramolecule #1: Bovine TRiC in complex with actin and CCT1 antibody
Supramolecule | Name: Bovine TRiC in complex with actin and CCT1 antibody / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Bos taurus (cattle) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 18.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
-Image processing
Startup model | Type of model: EMDB MAP EMDB ID: |
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Final reconstruction | Applied 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 assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |