[English] 日本語
Yorodumi- EMDB-62090: Structure of substrate-engaged double-cap human proteasome in sta... -
+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Structure of substrate-engaged double-cap human proteasome in state EA1-EA1 | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
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 / Formation of the ternary complex, and subsequently, the 43S complex / 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 / Ribosomal scanning and start codon recognition / proteasome binding / Translation initiation complex formation / Impaired BRCA2 binding to RAD51 / myofibril / regulation of protein catabolic process / proteasome storage granule / proteasomal ubiquitin-independent protein catabolic process / SARS-CoV-1 modulates host translation machinery / Peptide chain elongation / sperm head-tail coupling apparatus / Selenocysteine synthesis / Formation of a pool of free 40S subunits / general transcription initiation factor binding / Presynaptic phase of homologous DNA pairing and strand exchange / Eukaryotic Translation Termination / blastocyst development / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / protein deubiquitination / Viral mRNA Translation / polyubiquitin modification-dependent protein binding / immune system process / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / proteasome endopeptidase complex / NF-kappaB binding / GTP hydrolysis and joining of the 60S ribosomal subunit / proteasome core complex, beta-subunit complex / endopeptidase activator activity / L13a-mediated translational silencing of Ceruloplasmin expression / threonine-type endopeptidase activity / proteasome assembly / mRNA export from nucleus / proteasome core complex, alpha-subunit complex / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / enzyme regulator activity / regulation of proteasomal protein catabolic process / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / inclusion body / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling 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
| |||||||||
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 |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_62090.map.gz | 1.7 GB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-62090-v30.xml emd-62090.xml | 57.3 KB 57.3 KB | Display Display | EMDB header |
| Images | emd_62090.png | 68.6 KB | ||
| Filedesc metadata | emd-62090.cif.gz | 14.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62090 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62090 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9k5eMC ![]() 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 ![]() 9k5cC ![]() 9k5dC M: atomic model generated by this map C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|---|
| Related items in Molecule of the Month |
-
Map
| File | Download / File: emd_62090.map.gz / Format: CCP4 / Size: 1.9 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.685 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-
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: Ubiquitin
+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 |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Buffer | pH: 7 |
|---|---|
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| 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 |
Movie
Controller
About Yorodumi



Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation


























































































Z (Sec.)
Y (Row.)
X (Col.)






















Processing
FIELD EMISSION GUN
