- EMDB-2947: Cryo-electron microscopy structure of the occupied population of ... -
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Basic information
Entry
Database: EMDB / ID: EMD-2947
Title
Cryo-electron microscopy structure of the occupied population of CCT5 complexes (mutant huntington oligomer subtrate)
Map data
Single particle tomography reconstruction of CCT5 complex with mutant huntingtin encapsulated within its cavity.
Sample
Sample: CCT5 complex with encapsulated oligomeric mutant huntingtin exon 1.
Protein or peptide: chaperonin containing TCP1, subunit 5 (epsilon) complex
Protein or peptide: mutant huntington exon 1
Keywords
chaperonin / Huntington's disease / protein aggregation
Function / homology
Function and homology information
regulation of cAMP-dependent protein kinase activity / regulation of phosphoprotein phosphatase activity / positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity / microtubule-based transport / vocal learning / regulation of CAMKK-AMPK signaling cascade / positive regulation of mitophagy / profilin binding / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body ...regulation of cAMP-dependent protein kinase activity / regulation of phosphoprotein phosphatase activity / positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity / microtubule-based transport / vocal learning / regulation of CAMKK-AMPK signaling cascade / positive regulation of mitophagy / profilin binding / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / vesicle transport along microtubule / BBSome-mediated cargo-targeting to cilium / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / positive regulation of telomerase RNA localization to Cajal body / Formation of tubulin folding intermediates by CCT/TriC / positive regulation of cilium assembly / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-complex / presynaptic cytosol / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / positive regulation of aggrephagy / postsynaptic cytosol / positive regulation of lipophagy / dynein intermediate chain binding / beta-tubulin binding / Golgi organization / Association of TriC/CCT with target proteins during biosynthesis / establishment of mitotic spindle orientation / dynactin binding / Regulation of MECP2 expression and activity / autophagosome / chaperone-mediated protein folding / protein folding chaperone / inclusion body / positive regulation of telomere maintenance via telomerase / heat shock protein binding / centriole / mRNA 3'-UTR binding / negative regulation of extrinsic apoptotic signaling pathway / ATP-dependent protein folding chaperone / protein destabilization / response to virus / cytoplasmic vesicle membrane / mRNA 5'-UTR binding / kinase binding / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / unfolded protein binding / p53 binding / late endosome / protein folding / cell body / microtubule / transmembrane transporter binding / early endosome / protein stabilization / positive regulation of apoptotic process / axon / centrosome / apoptotic process / dendrite / perinuclear region of cytoplasm / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / protein-containing complex / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function
Journal: J Biol Chem / Year: 2014 Title: Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy. Authors: Oksana A Sergeeva / Meme T Tran / Cameron Haase-Pettingell / Jonathan A King / Abstract: Hereditary sensory neuropathies are a class of disorders marked by degeneration of the nerve fibers in the sensory periphery neurons. Recently, two mutations were identified in the subunits of the ...Hereditary sensory neuropathies are a class of disorders marked by degeneration of the nerve fibers in the sensory periphery neurons. Recently, two mutations were identified in the subunits of the eukaryotic cytosolic chaperonin TRiC, a protein machine responsible for folding actin and tubulin in the cell. C450Y CCT4 was identified in a stock of Sprague-Dawley rats, whereas H147R CCT5 was found in a human Moroccan family. As with many genetically identified mutations associated with neuropathies, the underlying molecular basis of the mutants was not defined. We investigated the biochemical properties of these mutants using an expression system in Escherichia coli that produces homo-oligomeric rings of CCT4 and CCT5. Full-length versions of both mutant protein chains were expressed in E. coli at levels approaching that of the WT chains. Sucrose gradient centrifugation revealed chaperonin-sized complexes of both WT and mutant chaperonins, but with reduced recovery of C450Y CCT4 soluble subunits. Electron microscopy of negatively stained samples of C450Y CCT4 revealed few ring-shaped species, whereas WT CCT4, H147R CCT5, and WT CCT5 revealed similar ring structures. CCT5 complexes were assayed for their ability to suppress aggregation of and refold the model substrate γd-crystallin, suppress aggregation of mutant huntingtin, and refold the physiological substrate β-actin in vitro. H147R CCT5 was not as efficient in chaperoning these substrates as WT CCT5. The subtle effects of these mutations are consistent with the homozygous disease phenotype, in which most functions are carried out during development and adulthood, but some selective function is lost or reduced.
History
Deposition
Mar 24, 2015
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Header (metadata) release
May 6, 2015
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Map release
Jun 3, 2015
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Update
Jul 22, 2015
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Current status
Jul 22, 2015
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Name: CCT5 complex with encapsulated oligomeric mutant huntingtin exon 1. type: sample / ID: 1000 Oligomeric state: 16 CCT5 subunits make up one CCT5 complex, which encapsulates a hetergeneous mixture of mutant huntingtin oligomeric species. Number unique components: 2
Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 95 K / Instrument: FEI VITROBOT MARK III Method: 1x or 2x double sided blotting for 1 or 2 second each blot before plunging.
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Electron microscopy #1
Microscopy ID
1
Microscope
JEOL 2200FS
Temperature
Average: 95 K
Specialist optics
Energy filter - Name: Gatan / Energy filter - Lower energy threshold: 0.0 eV / Energy filter - Upper energy threshold: 25.0 eV
Date
Feb 12, 2014
Image recording
Category: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Average electron dose: 2.0 e/Å2 / Camera length: 1200
Electron beam
Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
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