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Open data
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Basic information
| Entry | Database: PDB / ID: 9iwr | ||||||||||||||||||||||||
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| Title | 26S proteasome trimer | ||||||||||||||||||||||||
Components |
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Keywords | HYDROLASE / proteasome / trimer / complex / PSG / paracrystalline | ||||||||||||||||||||||||
| Function / homology | Function and homology informationSAGA complex localization to transcription regulatory region / : / proteasome regulatory particle assembly / proteasome storage granule assembly / transcription export complex 2 / peroxisome fission / protein deneddylation / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome ...SAGA complex localization to transcription regulatory region / : / proteasome regulatory particle assembly / proteasome storage granule assembly / transcription export complex 2 / peroxisome fission / protein deneddylation / maintenance of DNA trinucleotide repeats / filamentous growth / COP9 signalosome / proteasome regulatory particle / protein-containing complex localization / mitochondrial fission / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / K48-linked polyubiquitin modification-dependent protein binding / proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / nonfunctional rRNA decay / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / peptide catabolic process / proteasome binding / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / regulation of protein catabolic process / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of RNA polymerase II transcription preinitiation complex assembly / polyubiquitin modification-dependent protein binding / protein deubiquitination / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / Ub-specific processing proteases / endopeptidase activator activity / proteasome assembly / threonine-type endopeptidase activity / mRNA export from nucleus / proteasome core complex, alpha-subunit complex / enzyme regulator activity / ERAD pathway / Neutrophil degranulation / protein folding chaperone / proteasome complex / ubiquitin binding / nucleotide-excision repair / positive regulation of transcription elongation by RNA polymerase II / double-strand break repair via homologous recombination / metallopeptidase activity / positive regulation of protein catabolic process / peroxisome / ubiquitin-dependent protein catabolic process / endopeptidase activity / protein-macromolecule adaptor activity / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / regulation of cell cycle / chromatin remodeling / protein domain specific binding / mRNA binding / ubiquitin protein ligase binding / endoplasmic reticulum membrane / structural molecule activity / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / mitochondrion / ATP binding / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 9.1 Å | ||||||||||||||||||||||||
Authors | Qu, L. / Tang, X. | ||||||||||||||||||||||||
| Funding support | Germany, 2items
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Citation | Journal: To Be PublishedTitle: Metabolically regulated proteasome supramolecular organization Authors: Tang, X. / Qu, L. / Florian, W. / Oliver, P.E. / Brenda, A.S. / Baumeister, W. / Cordula, E. | ||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9iwr.cif.gz | 12.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9iwr.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9iwr.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iw/9iwr ftp://data.pdbj.org/pub/pdb/validation_reports/iw/9iwr | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 60960MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Number of models | 3 |
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Components
-Proteasome subunit beta type- ... , 7 types, 14 molecules 1h2i3j4k5l6m7n
| #1: Protein | Mass: 23573.604 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P38624, proteasome endopeptidase complex #2: Protein | Mass: 28299.889 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P25043, proteasome endopeptidase complex #3: Protein | Mass: 22627.842 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P25451, proteasome endopeptidase complex #4: Protein | Mass: 22545.676 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P22141, proteasome endopeptidase complex #5: Protein | Mass: 31670.539 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P30656, proteasome endopeptidase complex #6: Protein | Mass: 26905.076 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P23724, proteasome endopeptidase complex #7: Protein | Mass: 29471.289 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P30657, proteasome endopeptidase complex |
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-Proteasome subunit alpha type- ... , 6 types, 12 molecules AaBbCcDdEeFf
| #8: Protein | Mass: 28033.830 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P21243, proteasome endopeptidase complex #9: Protein | Mass: 27191.828 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P23639, proteasome endopeptidase complex #10: Protein | Mass: 28748.230 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P23638, proteasome endopeptidase complex #11: Protein | Mass: 28478.111 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P40303, proteasome endopeptidase complex #12: Protein | Mass: 28649.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P32379, proteasome endopeptidase complex #13: Protein | Mass: 25634.000 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P40302, proteasome endopeptidase complex |
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-Protein , 4 types, 5 molecules GgLVY
| #14: Protein | Mass: 31575.068 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P21242, proteasome endopeptidase complex #19: Protein | | Mass: 49480.137 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #29: Protein | | Mass: 34442.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #32: Protein | | Mass: 10397.102 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-26S protease regulatory subunit ... , 5 types, 5 molecules HIJKM
| #15: Protein | Mass: 52054.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #16: Protein | Mass: 48898.160 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #17: Protein | Mass: 45342.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #18: Protein | Mass: 47953.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #20: Protein | Mass: 48315.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-26S proteasome regulatory subunit ... , 11 types, 11 molecules NOPQRSTUWXZ
| #21: Protein | Mass: 104351.883 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #22: Protein | Mass: 45839.348 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #23: Protein | Mass: 51840.352 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #24: Protein | Mass: 49839.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #25: Protein | Mass: 49016.367 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #26: Protein | Mass: 60464.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #27: Protein | Mass: 31952.119 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #28: Protein | Mass: 38365.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #30: Protein | Mass: 29776.098 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #31: Protein | Mass: 17919.002 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #33: Protein | Mass: 109601.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Details
| Has protein modification | N |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
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Sample preparation
| Component | Name: 26S proteasome trimer / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 6.8 / Details: YPD buffer |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| 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: 4000 nm / Nominal defocus min: 3000 nm |
| Image recording | Electron dose: 2.7 e/Å2 / Avg electron dose per subtomogram: 100 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| Symmetry | Point symmetry: D3 (2x3 fold dihedral) |
| 3D reconstruction | Resolution: 9.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1700 / Symmetry type: POINT |
| EM volume selection | Num. of tomograms: 73 / Num. of volumes extracted: 1700 |
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FIELD EMISSION GUN