+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0496 | ||||||||||||||||||||||||
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Title | hTRiC-hPFD all particles | ||||||||||||||||||||||||
Map data | hTRiC-hPFD all particles | ||||||||||||||||||||||||
Sample |
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Function / homology | Function and homology information RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / scaRNA localization to Cajal body / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / chaperone mediated protein folding independent of cofactor / RNA polymerase II core complex assembly ...RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / scaRNA localization to Cajal body / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / chaperone mediated protein folding independent of cofactor / RNA polymerase II core complex assembly / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / RPAP3/R2TP/prefoldin-like complex / binding of sperm to zona pellucida / positive regulation of telomerase RNA localization to Cajal body / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / chaperonin-containing T-complex / Prefoldin mediated transfer of substrate to CCT/TriC / negative regulation of amyloid fibril formation / protein folding chaperone complex / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / pericentriolar material / beta-tubulin binding / Association of TriC/CCT with target proteins during biosynthesis / : / microtubule-based process / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / positive regulation of telomere maintenance via telomerase / protein folding chaperone / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / tubulin binding / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / negative regulation of canonical Wnt signaling pathway / cilium / mRNA 5'-UTR binding / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / transcription corepressor activity / azurophil granule lumen / G-protein beta-subunit binding / unfolded protein binding / melanosome / protein folding / retina development in camera-type eye / protein-folding chaperone binding / amyloid-beta binding / cell body / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / cytoskeleton / protein stabilization / cadherin binding / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of DNA-templated transcription / Golgi apparatus / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.5 Å | ||||||||||||||||||||||||
Authors | Gestaut DR / Roh SH | ||||||||||||||||||||||||
Funding support | United States, Germany, 7 items
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Citation | Journal: Cell / Year: 2019 Title: The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis. Authors: Daniel Gestaut / Soung Hun Roh / Boxue Ma / Grigore Pintilie / Lukasz A Joachimiak / Alexander Leitner / Thomas Walzthoeni / Ruedi Aebersold / Wah Chiu / Judith Frydman / Abstract: Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the ...Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis. | ||||||||||||||||||||||||
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_0496.map.gz | 49 MB | EMDB map data format | |
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Header (meta data) | emd-0496-v30.xml emd-0496.xml | 17.8 KB 17.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_0496_fsc.xml | 8.2 KB | Display | FSC data file |
Images | emd_0496.png | 60.8 KB | ||
Others | emd_0496_additional.map.gz emd_0496_half_map_1.map.gz emd_0496_half_map_2.map.gz | 40 MB 40.7 MB 40.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0496 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0496 | HTTPS FTP |
-Validation report
Summary document | emd_0496_validation.pdf.gz | 78.7 KB | Display | EMDB validaton report |
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Full document | emd_0496_full_validation.pdf.gz | 77.9 KB | Display | |
Data in XML | emd_0496_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0496 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0496 | HTTPS FTP |
-Related structure data
Related structure data | 0490C 0491C 0492C 0493C 0494C 0495C 6nr8C 6nr9C 6nraC 6nrbC 6nrcC 6nrdC C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_0496.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | hTRiC-hPFD all particles | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: hTRiC-hPFD all particles, unfiltered sum map
File | emd_0496_additional.map | ||||||||||||
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Annotation | hTRiC-hPFD all particles, unfiltered sum map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: hTRiC-hPFD all particles, half map 1
File | emd_0496_half_map_1.map | ||||||||||||
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Annotation | hTRiC-hPFD all particles, half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: hTRiC-hPFD all particles, half map 2
File | emd_0496_half_map_2.map | ||||||||||||
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Annotation | hTRiC-hPFD all particles, half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : hTRiC-hPFD
Entire | Name: hTRiC-hPFD |
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Components |
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-Supramolecule #1: hTRiC-hPFD
Supramolecule | Name: hTRiC-hPFD / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Insect cell expression vector pTIE1 (others) |
-Supramolecule #2: hTRiC
Supramolecule | Name: hTRiC / type: complex / ID: 2 / Parent: 1 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Insect cell expression vector pTIE1 (others) |
-Supramolecule #3: hPFD
Supramolecule | Name: hPFD / type: complex / ID: 3 / Parent: 1 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Insect cell expression vector pTIE1 (others) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | JEOL 3200FSC |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 1.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |