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Open data
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Basic information
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Title | CCT G beta 5 complex closed state 13 | |||||||||
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![]() | CCT / Gb5 / complex / open / CHAPERONE | |||||||||
Function / homology | ![]() heterotrimeric G-protein complex assembly / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere ...heterotrimeric G-protein complex assembly / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / binding of sperm to zona pellucida / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / cell projection organization / positive regulation of telomerase RNA localization to Cajal body / regulation of G protein-coupled receptor signaling pathway / chaperonin-containing T-complex / Prefoldin mediated transfer of substrate to CCT/TriC / positive regulation of smoothened signaling pathway / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / G protein-coupled dopamine receptor signaling pathway / pericentriolar material / beta-tubulin binding / Association of TriC/CCT with target proteins during biosynthesis / : / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomere maintenance via telomerase / visual perception / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / GTPase activator activity / acrosomal vesicle / positive regulation of GTPase activity / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / cilium / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / mRNA 5'-UTR binding / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / G-protein beta-subunit binding / Inactivation, recovery and regulation of the phototransduction cascade / heterotrimeric G-protein complex / azurophil granule lumen / G alpha (12/13) signalling events / unfolded protein binding / melanosome / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / protein folding / presynapse / Ca2+ pathway / protein-folding chaperone binding / G alpha (i) signalling events / cell body / G alpha (s) signalling events / G alpha (q) signalling events / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / Extra-nuclear estrogen signaling / cytoskeleton / protein stabilization / cadherin binding / G protein-coupled receptor signaling pathway / GTPase activity / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / Golgi apparatus / signal transduction / ATP hydrolysis activity / RNA binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
![]() | Wang S / Sass M / Willardson BM / Shen PS | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller. Authors: Shuxin Wang / Mikaila I Sass / Yujin Kwon / W Grant Ludlam / Theresa M Smith / Ethan J Carter / Nathan E Gladden / Margot Riggi / Janet H Iwasa / Barry M Willardson / Peter S Shen / ![]() Abstract: The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, ...The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gβ, a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gβ from an unfolded molten globule to a fully folded β-propeller. These structures reveal the mechanism by which CCT directs Gβ folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual β sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 50.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 30.1 KB 30.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.9 KB | Display | ![]() |
Images | ![]() | 528.1 KB | ||
Filedesc metadata | ![]() | 9.2 KB | ||
Others | ![]() ![]() | 73.1 MB 73.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8shpMC ![]() 8sfeC ![]() 8sffC ![]() 8sg8C ![]() 8sg9C ![]() 8sgcC ![]() 8sglC ![]() 8sgqC ![]() 8sh9C ![]() 8shaC ![]() 8shdC ![]() 8sheC ![]() 8shfC ![]() 8shgC ![]() 8shlC ![]() 8shnC ![]() 8shoC ![]() 8shqC ![]() 8shtC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.058 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_40491_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_40491_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : CCT-Gb5-PhLP1 in closed state 13
+Supramolecule #1: CCT-Gb5-PhLP1 in closed state 13
+Macromolecule #1: Guanine nucleotide-binding protein subunit beta-5
+Macromolecule #2: T-complex protein 1 subunit alpha
+Macromolecule #3: T-complex protein 1 subunit beta
+Macromolecule #4: T-complex protein 1 subunit delta
+Macromolecule #5: T-complex protein 1 subunit epsilon
+Macromolecule #6: T-complex protein 1 subunit gamma
+Macromolecule #7: T-complex protein 1 subunit eta, N-terminally processed
+Macromolecule #8: T-complex protein 1 subunit theta
+Macromolecule #9: T-complex protein 1 subunit zeta
+Macromolecule #10: Phosducin-like protein
+Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #12: MAGNESIUM ION
+Macromolecule #13: ALUMINUM FLUORIDE
+Macromolecule #14: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.5 mg/mL | |||||||||||||||||||||
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Buffer | pH: 7.5 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK I | |||||||||||||||||||||
Details | The sample was monodisperse |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.42 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |