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Yorodumi- EMDB-62088: Structure of substrate-engaged single-cap human proteasome in sta... -
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Basic information
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| Title | Structure of substrate-engaged single-cap human proteasome in state ED1 | |||||||||
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Keywords | Proteasome / AAA-ATPase / Deubiquitinase / HYDROLASE | |||||||||
| Function / homology | Function and homology informationthyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / positive regulation of inclusion body assembly / proteasome accessory complex / meiosis I / integrator complex / purine ribonucleoside triphosphate binding ...thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / positive regulation of inclusion body assembly / proteasome accessory complex / meiosis I / integrator complex / purine ribonucleoside triphosphate binding / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / Antigen processing: Ub, ATP-independent proteasomal degradation / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / sperm glycocalyx / protein K63-linked deubiquitination / negative regulation of programmed cell death / metal-dependent deubiquitinase activity / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / proteasome core complex / perinuclear theca / Cross-presentation of soluble exogenous antigens (endosomes) / K63-linked deubiquitinase activity / Somitogenesis / transcription factor binding / 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) / Resolution of D-loop Structures through Holliday Junction Intermediates / proteasome binding / Impaired BRCA2 binding to RAD51 / myofibril / regulation of protein catabolic process / proteasome storage granule / proteasomal ubiquitin-independent protein catabolic process / sperm head-tail coupling apparatus / general transcription initiation factor binding / Presynaptic phase of homologous DNA pairing and strand exchange / blastocyst development / protein deubiquitination / polyubiquitin modification-dependent protein binding / immune system process / proteasome endopeptidase complex / NF-kappaB binding / proteasome core complex, beta-subunit complex / endopeptidase activator activity / threonine-type endopeptidase activity / proteasome assembly / mRNA export from nucleus / proteasome core complex, alpha-subunit complex / enzyme regulator activity / regulation of proteasomal protein catabolic process / inclusion body / TBP-class protein binding / : / ciliary tip / proteasome complex / stem cell differentiation / Regulation of activated PAK-2p34 by proteasome mediated degradation / sarcomere / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / ubiquitin binding / Asymmetric localization of PCP proteins / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / centriole / sperm end piece / negative regulation of inflammatory response to antigenic stimulus / P-body / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / lipopolysaccharide binding / 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 / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Hedgehog 'on' state Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
Authors | Wu Z / Chen E / Mao Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: To be publishedTitle: Hidden dynamics of ubiquitin-mediated proteasome autoregulation during protein degradation Authors: Wu Z / Chen E / Zou S / Hou Y / Zhang S / Wang W / Dong Y / Mao Y | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_62088.map.gz | 747.9 MB | EMDB map data format | |
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| Header (meta data) | emd-62088-v30.xml emd-62088.xml | 60.4 KB 60.4 KB | Display Display | EMDB header |
| Images | emd_62088.png | 80.3 KB | ||
| Filedesc metadata | emd-62088.cif.gz | 14.5 KB | ||
| Others | emd_62088_half_map_1.map.gz emd_62088_half_map_2.map.gz | 732.8 MB 733.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62088 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62088 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9k5cMC ![]() 9k4jC ![]() 9k4kC ![]() 9k4lC ![]() 9k4mC ![]() 9k4oC ![]() 9k4pC ![]() 9k4rC ![]() 9k4sC ![]() 9k4tC ![]() 9k4uC ![]() 9k4vC ![]() 9k4wC ![]() 9k4xC ![]() 9k4yC ![]() 9k4zC ![]() 9k50C ![]() 9k51C ![]() 9k53C ![]() 9k54C ![]() 9k55C ![]() 9k56C ![]() 9k57C ![]() 9k58C ![]() 9k59C ![]() 9k5aC ![]() 9k5bC ![]() 9k5dC ![]() 9k5eC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_62088.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.685 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_62088_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_62088_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : 26S proteasome
+Supramolecule #1: 26S proteasome
+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: Proteasome 26S subunit, ATPase 6
+Macromolecule #6: 26S proteasome regulatory subunit 6A
+Macromolecule #7: Proteasome subunit alpha type-6
+Macromolecule #8: Proteasome subunit alpha type-2
+Macromolecule #9: Proteasome subunit alpha type-4
+Macromolecule #10: Proteasome subunit alpha type-7
+Macromolecule #11: Proteasome subunit alpha type-5
+Macromolecule #12: Proteasome subunit alpha type-1
+Macromolecule #13: Proteasome subunit alpha type-3
+Macromolecule #14: Proteasome subunit beta type-6
+Macromolecule #15: Proteasome subunit beta type-7
+Macromolecule #16: Proteasome subunit beta type-3
+Macromolecule #17: Proteasome subunit beta type-2
+Macromolecule #18: Proteasome subunit beta type-5
+Macromolecule #19: Proteasome subunit beta type-1
+Macromolecule #20: Proteasome subunit beta type-4
+Macromolecule #21: 26S proteasome non-ATPase regulatory subunit 1
+Macromolecule #22: 26S proteasome non-ATPase regulatory subunit 3
+Macromolecule #23: 26S proteasome non-ATPase regulatory subunit 12
+Macromolecule #24: 26S proteasome non-ATPase regulatory subunit 11
+Macromolecule #25: 26S proteasome non-ATPase regulatory subunit 6
+Macromolecule #26: 26S proteasome non-ATPase regulatory subunit 7
+Macromolecule #27: 26S proteasome non-ATPase regulatory subunit 13
+Macromolecule #28: 26S proteasome non-ATPase regulatory subunit 4
+Macromolecule #29: 26S proteasome non-ATPase regulatory subunit 14
+Macromolecule #30: 26S proteasome non-ATPase regulatory subunit 8
+Macromolecule #31: 26S proteasome complex subunit SEM1
+Macromolecule #32: 26S proteasome non-ATPase regulatory subunit 2
+Macromolecule #33: Substrate
+Macromolecule #34: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #35: MAGNESIUM ION
+Macromolecule #36: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #37: 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 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 44.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
China, 1 items
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Y (Row.)
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Processing
FIELD EMISSION GUN
