+Open data
-Basic information
Entry | Database: PDB / ID: 8hki | ||||||
---|---|---|---|---|---|---|---|
Title | Human TRiC open state | ||||||
Components | (T-complex protein 1 subunit ...) x 8 | ||||||
Keywords | STRUCTURAL PROTEIN / TRiC / cryo-EM | ||||||
Function / homology | Function and homology information 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 / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Formation of tubulin folding intermediates by CCT/TriC ...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 / 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 / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-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 / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / : / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / cilium / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / azurophil granule lumen / unfolded protein binding / melanosome / protein folding / cell body / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / cytoskeleton / protein stabilization / cadherin binding / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||
Authors | Cong, Y. / Liu, C.X. | ||||||
Funding support | China, 1items
| ||||||
Citation | Journal: To Be Published Title: Pathway and mechanism of tubulin folding mediated by TRiC/CCT conjugated with its ATPase cycle revealed by cryo-EM Authors: Cong, Y. / Liu, C.X. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8hki.cif.gz | 801.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8hki.ent.gz | 629.6 KB | Display | PDB format |
PDBx/mmJSON format | 8hki.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8hki_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8hki_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 8hki_validation.xml.gz | 107.4 KB | Display | |
Data in CIF | 8hki_validation.cif.gz | 166.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hk/8hki ftp://data.pdbj.org/pub/pdb/validation_reports/hk/8hki | HTTPS FTP |
-Related structure data
Related structure data | 34852MC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
-T-complex protein 1 subunit ... , 8 types, 16 molecules aAbBDdEegGhHQqZz
#1: Protein | Mass: 60418.477 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TCP1, CCT1, CCTA / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P17987 #2: Protein | Mass: 57567.141 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT2, 99D8.1, CCTB / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P78371 #3: Protein | Mass: 57996.113 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT4, CCTD, SRB / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P50991 #4: Protein | Mass: 59547.684 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT5, CCTE, KIAA0098 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P48643 #5: Protein | Mass: 60613.855 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT3, CCTG, TRIC5 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P49368 #6: Protein | Mass: 59417.457 Da / Num. of mol.: 2 / Mutation: L291S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT7 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q99832 #7: Protein | Mass: 59691.422 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT8, C21orf112, CCTQ / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P50990 #8: Protein | Mass: 58106.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCT6A, CCT6, CCTZ / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P40227 |
---|
-Non-polymers , 1 types, 6 molecules
#9: Chemical | ChemComp-ADP / |
---|
-Details
Has ligand of interest | Y |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Cryo-EM structure of human TRiC at open state / Type: COMPLEX / Entity ID: #1-#8 / Source: NATURAL |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Insecta environmental sample (insect) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 38 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
---|---|
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 185216 / Symmetry type: POINT |