- 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
Title
Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound
Map data
Sample
Complex: Human type II chaperonin TRiC/CCT complex with nanobody Nb18, actin and PhLP2A bound
Complex: Human type II chaperonin TRiC/CCT
Protein or peptide: x 8 types
Complex: T-complex protein
Protein or peptide: x 2 types
Complex: Nanobody
Protein or peptide: x 1 types
Ligand: x 4 types
Function / homology
Function and homology information
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 / regulation of synaptic vesicle endocytosis / RHOBTB1 GTPase cycle / 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 / protein folding chaperone / regulation of peptidyl-tyrosine phosphorylation / 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 / negative regulation of ubiquitin-dependent protein catabolic process / phagocytic vesicle / 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 / ATP-dependent protein folding chaperone / FCGR3A-mediated phagocytosis / 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 / cilium / mRNA 5'-UTR binding / 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
Phosducin, thioredoxin-like domain / Phosducin / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit ...Phosducin, thioredoxin-like domain / Phosducin / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / Thioredoxin-like superfamily Similarity search - Domain/homology
T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / Actin, cytoplasmic 2 / T-complex protein 1 subunit beta / T-complex protein 1 subunit eta / Phosducin-like protein 3 Similarity search - Component
Biological species
Homo sapiens (human) / Lama glama (llama) / Human (human)
Method
single particle reconstruction / cryo EM / Resolution: 3.1 Å
Journal: Nat Struct Mol Biol / Year: 2022 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
Deposition
Mar 15, 2021
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Header (metadata) release
Mar 2, 2022
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Map release
Mar 2, 2022
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Update
Jun 1, 2022
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Current status
Jun 1, 2022
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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