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Yorodumi- PDB-9rkz: CryoEM structure of human 20S proteasome in complex with proteaso... -
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Basic information
| Entry | Database: PDB / ID: 9rkz | ||||||||||||||||||||||||||||||
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| Title | CryoEM structure of human 20S proteasome in complex with proteasome inhibitor CP-17 | ||||||||||||||||||||||||||||||
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Keywords | HYDROLASE | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationpurine ribonucleoside triphosphate binding / Antigen processing: Ub, ATP-independent proteasomal degradation / sperm glycocalyx / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / proteasome core complex / perinuclear theca / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / myofibril ...purine ribonucleoside triphosphate binding / Antigen processing: Ub, ATP-independent proteasomal degradation / sperm glycocalyx / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / proteasome core complex / perinuclear theca / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / myofibril / proteasomal ubiquitin-independent protein catabolic process / sperm head-tail coupling apparatus / immune system process / proteasome endopeptidase complex / NF-kappaB binding / proteasome core complex, beta-subunit complex / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / proteasome assembly / : / ciliary tip / proteasome complex / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / centriole / APC/C:Cdc20 mediated degradation of Securin / sperm end piece / negative regulation of inflammatory response to antigenic stimulus / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / lipopolysaccharide binding / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / P-body / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of DVL / Degradation of AXIN / Degradation of CRY and PER proteins / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / G2/M Checkpoints / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Regulation of RUNX3 expression and activity / Autodegradation of the E3 ubiquitin ligase COP1 / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Hedgehog 'on' state / Vif-mediated degradation of APOBEC3G / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / MAPK6/MAPK4 signaling / Degradation of CDH1 / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / ABC-family protein mediated transport / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / response to virus / FCERI mediated NF-kB activation / nuclear matrix / Regulation of expression of SLITs and ROBOs / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RUNX2 expression and activity / Regulation of RAS by GAPs / The role of GTSE1 in G2/M progression after G2 checkpoint / Separation of Sister Chromatids / UCH proteinases / KEAP1-NFE2L2 pathway / peptidase activity / Downstream TCR signaling / Antigen processing: Ubiquitination & Proteasome degradation / sperm principal piece / RUNX1 regulates transcription of genes involved in differentiation of HSCs / ER-Phagosome pathway / Neddylation / regulation of inflammatory response / response to oxidative stress / sperm midpiece / secretory granule lumen / endopeptidase activity / ficolin-1-rich granule lumen / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / Ub-specific processing proteases / cilium / nuclear body Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.95 Å | ||||||||||||||||||||||||||||||
Authors | Benova, V. / Suelzen, H. / Boura, E. / Silhan, J. / Fajtova, P. | ||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: CryoEM structure of human 20S proteasome in complex with proteasome inhibitor CP-17 Authors: Benova, V. / Suelzen, H. / Boura, E. / Silhan, J. / Fajtova, P. | ||||||||||||||||||||||||||||||
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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 | 9rkz.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9rkz.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9rkz.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rk/9rkz ftp://data.pdbj.org/pub/pdb/validation_reports/rk/9rkz | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54027MC 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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Components
-Proteasome subunit alpha type- ... , 7 types, 14 molecules AOBPCQERFSGTDZ
| #1: Protein | Mass: 27432.459 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA6, PROS27Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P60900 #2: Protein | Mass: 25927.535 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA2, HC3, PSC3Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P25787, proteasome endopeptidase complex #3: Protein | Mass: 29525.842 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA4, HC9, PSC9Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P25789, proteasome endopeptidase complex #4: Protein | Mass: 26435.977 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA5Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P28066, proteasome endopeptidase complex #5: Protein | Mass: 29595.627 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA1, HC2, NU, PROS30, PSC2Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P25786 #6: Protein | Mass: 28469.252 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA3, HC8, PSC8Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P25788, proteasome endopeptidase complex #11: Protein | Mass: 27929.891 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA7, HSPCProduction host: Homo sapiens environmental sample (environmental samples)References: UniProt: O14818 |
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-Proteasome subunit beta type- ... , 7 types, 14 molecules JVKWMXNYHaIbLc
| #7: Protein | Mass: 22841.701 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB3Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P49720, proteasome endopeptidase complex #8: Protein | Mass: 22864.277 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB2Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P49721, proteasome endopeptidase complex #9: Protein | Mass: 23578.986 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB1, PSC5Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P20618, proteasome endopeptidase complex #10: Protein | Mass: 24414.740 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB4, PROS26Production host: Homo sapiens environmental sample (environmental samples)References: UniProt: P28070, proteasome endopeptidase complex #12: Protein | Mass: 21921.836 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB6, LMPY, YProduction host: Homo sapiens environmental sample (environmental samples)References: UniProt: P28072, proteasome endopeptidase complex #13: Protein | Mass: 25321.980 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB7, ZProduction host: Homo sapiens environmental sample (environmental samples)References: UniProt: Q99436, proteasome endopeptidase complex #14: Protein | Mass: 22142.020 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PSMB5, LMPX, MB1, XProduction host: Homo sapiens environmental sample (environmental samples)References: UniProt: P28074, proteasome endopeptidase complex |
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-Non-polymers , 1 types, 2 molecules
| #15: Chemical | Mass: 679.848 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C40H49N5O5 / Feature type: SUBJECT OF INVESTIGATION |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: CryoEM structure of human 20S proteasome in complex with proteasome inhibitor CP-17 Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1-#14 / Source: NATURAL | ||||||||||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||
| Buffer component |
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| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: 50 micromolar CP-17 | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 0 % |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 2.95 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 254452 / Symmetry type: POINT |
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