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Yorodumi- EMDB-8675: Conformational Landscape of the p28-Bound Human Proteasome Regula... -
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Basic information
| Entry | Database: EMDB / ID: EMD-8675 | |||||||||
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| Title | Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle | |||||||||
Map data | Final map of human proteasome RP in the T2 state corrected with a B-factor of -120 | |||||||||
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Keywords | p28 / 26S proteasome / regulatory particle / 19S / gankyrin / HYDROLASE | |||||||||
| Function / homology | Function and homology informationproteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / positive regulation of cyclin-dependent protein serine/threonine kinase activity / proteasome accessory complex ...proteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / positive regulation of cyclin-dependent protein serine/threonine kinase activity / proteasome accessory complex / integrator complex / meiosis I / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / protein K63-linked deubiquitination / negative regulation of programmed cell death / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Somitogenesis / Resolution of D-loop Structures through Holliday Junction Intermediates / K63-linked deubiquitinase activity / negative regulation of NF-kappaB transcription factor activity / Impaired BRCA2 binding to RAD51 / proteasome binding / transcription factor binding / negative regulation of release of cytochrome c from mitochondria / regulation of protein catabolic process / negative regulation of DNA damage response, signal transduction by p53 class mediator / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / general transcription initiation factor binding / blastocyst development / positive regulation of RNA polymerase II transcription preinitiation complex assembly / polyubiquitin modification-dependent protein binding / protein deubiquitination / endopeptidase activator activity / mRNA export from nucleus / proteasome assembly / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / negative regulation of MAPK cascade / enzyme regulator activity / regulation of proteasomal protein catabolic process / ERAD pathway / inclusion body / TBP-class protein binding / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / positive regulation of protein ubiquitination / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / stem cell differentiation / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of AXIN / P-body / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / G2/M Checkpoints / Hedgehog ligand biogenesis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Defective CFTR causes cystic fibrosis / Autodegradation of the E3 ubiquitin ligase COP1 / Negative regulation of NOTCH4 signaling / Regulation of RUNX3 expression and activity / Vif-mediated degradation of APOBEC3G / Hedgehog 'on' state / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / MAPK6/MAPK4 signaling / double-strand break repair via homologous recombination / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ABC-family proteins mediated transport / HDR through Homologous Recombination (HRR) / double-strand break repair via nonhomologous end joining Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.1 Å | |||||||||
Authors | Lu Y / Wu J | |||||||||
Citation | Journal: Mol Cell / Year: 2017Title: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle. Authors: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao / ![]() Abstract: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly. | |||||||||
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Structure visualization
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_8675.map.gz | 57.4 MB | EMDB map data format | |
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| Header (meta data) | emd-8675-v30.xml emd-8675.xml | 37.4 KB 37.4 KB | Display Display | EMDB header |
| Images | emd_8675.png | 74.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8675 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8675 | HTTPS FTP |
-Validation report
| Summary document | emd_8675_validation.pdf.gz | 564 KB | Display | EMDB validaton report |
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| Full document | emd_8675_full_validation.pdf.gz | 563.5 KB | Display | |
| Data in XML | emd_8675_validation.xml.gz | 6 KB | Display | |
| Data in CIF | emd_8675_validation.cif.gz | 6.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8675 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8675 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5vhhMC ![]() 8672C ![]() 8674C ![]() 8676C ![]() 8677C ![]() 8678C ![]() 8679C ![]() 8680C ![]() 8681C ![]() 8682C ![]() 8683C ![]() 8684C ![]() 5vgzC ![]() 5vhfC ![]() 5vhiC ![]() 5vhjC ![]() 5vhmC ![]() 5vhnC ![]() 5vhoC ![]() 5vhpC ![]() 5vhqC ![]() 5vhrC ![]() 5vhsC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | |
| EM raw data | EMPIAR-10091 (Title: Conformational Landscape of the p28-Bound Human Proteasome Regulatory ParticleData size: 70.0 Data #1: Classified single-particle datasets for multiple conformations of p28-bound human regulatory complex [picked particles - multiframe - processed]) |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_8675.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Final map of human proteasome RP in the T2 state corrected with a B-factor of -120 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.98 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : Proteasome regulatory particle
+Supramolecule #1: Proteasome regulatory particle
+Macromolecule #1: 26S proteasome regulatory subunit 7
+Macromolecule #2: 26S proteasome regulatory subunit 4
+Macromolecule #3: 26S proteasome regulatory subunit 8
+Macromolecule #4: 26S proteasome regulatory subunit 6B
+Macromolecule #5: 26S proteasome regulatory subunit 10B
+Macromolecule #6: 26S proteasome regulatory subunit 6A
+Macromolecule #7: 26S proteasome non-ATPase regulatory subunit 1
+Macromolecule #8: 26S proteasome non-ATPase regulatory subunit 3
+Macromolecule #9: 26S proteasome non-ATPase regulatory subunit 12
+Macromolecule #10: 26S proteasome non-ATPase regulatory subunit 11
+Macromolecule #11: 26S proteasome non-ATPase regulatory subunit 6
+Macromolecule #12: 26S proteasome non-ATPase regulatory subunit 7
+Macromolecule #13: 26S proteasome non-ATPase regulatory subunit 13
+Macromolecule #14: 26S proteasome non-ATPase regulatory subunit 4
+Macromolecule #15: 26S proteasome non-ATPase regulatory subunit 14
+Macromolecule #16: 26S proteasome non-ATPase regulatory subunit 8
+Macromolecule #17: 26S proteasome complex subunit SEM1
+Macromolecule #18: 26S proteasome non-ATPase regulatory subunit 10
+Macromolecule #19: 26S proteasome non-ATPase regulatory subunit 2
+Macromolecule #20: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | 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 | FEI TECNAI ARCTICA |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: INSILICO MODEL |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 27629 |
| Initial angle assignment | Type: ANGULAR RECONSTITUTION |
| Final angle assignment | Type: PROJECTION MATCHING |
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Keywords
Homo sapiens (human)
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