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- EMDB-12606: Human TRiC complex in closed state with nanobody Nb18, actin and ... -
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Basic information
Entry | Database: EMDB / ID: EMD-12606 | |||||||||
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Title | Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound | |||||||||
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Function / homology | ![]() basal body patch / negative regulation of chaperone-mediated protein folding / perinucleolar compartment / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / structural constituent of postsynaptic actin cytoskeleton ...basal body patch / negative regulation of chaperone-mediated protein folding / perinucleolar compartment / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / structural constituent of postsynaptic actin cytoskeleton / profilin binding / positive regulation of establishment of protein localization to telomere / protein localization to bicellular tight junction / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Formation of tubulin folding intermediates by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / vascular endothelial growth factor receptor 2 binding / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-complex / Adherens junctions interactions / regulation of stress fiber assembly / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / RHOBTB1 GTPase cycle / regulation of synaptic vesicle endocytosis / intermediate filament cytoskeleton / WD40-repeat domain binding / apical junction complex / regulation of focal adhesion assembly / positive regulation of wound healing / maintenance of blood-brain barrier / myofibril / sarcomere organization / NuA4 histone acetyltransferase complex / pericentriolar material / beta-tubulin binding / Recycling pathway of L1 / Association of TriC/CCT with target proteins during biosynthesis / filamentous actin / calyx of Held / chaperone-mediated protein complex assembly / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / regulation of peptidyl-tyrosine phosphorylation / protein folding chaperone / positive regulation of telomerase activity / positive regulation of endothelial cell proliferation / positive regulation of telomere maintenance via telomerase / EPHB-mediated forward signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / phagocytic vesicle / negative regulation of ubiquitin-dependent protein catabolic process / axonogenesis / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / FCGR3A-mediated phagocytosis / ATP-dependent protein folding chaperone / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / response to virus / MAP2K and MAPK activation / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / mRNA 5'-UTR binding / cilium / platelet aggregation / VEGFA-VEGFR2 Pathway / cellular response to type II interferon / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / positive regulation of angiogenesis / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / G-protein beta-subunit binding / azurophil granule lumen / Signaling by BRAF and RAF1 fusions / cell-cell junction / unfolded protein binding / melanosome / protein folding Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
![]() | Kelly JJ / Chi G / Bulawa C / Paavilainen VO / Bountra C / Huiskonen JT / Yue W / Structural Genomics Consortium (SGC) | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Snapshots of actin and tubulin folding inside the TRiC chaperonin. Authors: John J Kelly / Dale Tranter / Els Pardon / Gamma Chi / Holger Kramer / Lotta Happonen / Kelly M Knee / Jay M Janz / Jan Steyaert / Christine Bulawa / Ville O Paavilainen / Juha T Huiskonen / Wyatt W Yue / ![]() ![]() ![]() ![]() ![]() Abstract: The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, ...The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC. | |||||||||
History |
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Structure visualization
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 229 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 31.3 KB 31.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.2 KB | Display | ![]() |
Images | ![]() | 213 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Others | ![]() ![]() | 194.1 MB 194.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1001.5 KB | Display | ![]() |
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Full document | ![]() | 1001 KB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 28.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7nvmMC ![]() 7nvlC ![]() 7nvnC ![]() 7nvoC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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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: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_12606_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_12606_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Human type II chaperonin TRiC/CCT complex with nanobody Nb18, act...
+Supramolecule #1: Human type II chaperonin TRiC/CCT complex with nanobody Nb18, act...
+Supramolecule #2: Human type II chaperonin TRiC/CCT
+Supramolecule #3: T-complex protein
+Supramolecule #4: Nanobody
+Macromolecule #1: T-complex protein 1 subunit alpha
+Macromolecule #2: T-complex protein 1 subunit beta
+Macromolecule #3: T-complex protein 1 subunit delta
+Macromolecule #4: T-complex protein 1 subunit epsilon
+Macromolecule #5: T-complex protein 1 subunit gamma
+Macromolecule #6: T-complex protein 1 subunit eta
+Macromolecule #7: Nanobody Nb18
+Macromolecule #8: T-complex protein 1 subunit theta
+Macromolecule #9: T-complex protein 1 subunit zeta
+Macromolecule #10: Actin, cytoplasmic 2
+Macromolecule #11: Phosducin-like protein 3
+Macromolecule #12: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #13: MAGNESIUM ION
+Macromolecule #14: ALUMINUM FLUORIDE
+Macromolecule #15: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 43.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |