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Yorodumi- EMDB-9512: Cryo-EM map of the human 26S proteasome at 3.5A resolution with C... -
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Basic information
| Entry | Database: EMDB / ID: EMD-9512 | ||||||||||||
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| Title | Cryo-EM map of the human 26S proteasome at 3.5A resolution with C2 symmetry | ||||||||||||
Map data | with C2 symmetry | ||||||||||||
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Keywords | protein complex / human proteasome / HYDROLASE | ||||||||||||
| Function / homology | Function and homology informationthyrotropin-releasing hormone receptor binding / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / proteasome accessory complex / integrator complex / meiosis I ...thyrotropin-releasing hormone receptor binding / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / proteasome accessory complex / integrator complex / meiosis I / purine ribonucleoside triphosphate binding / Antigen processing: Ub, ATP-independent proteasomal degradation / 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 / protein K63-linked deubiquitination / negative regulation of programmed cell death / Regulation of ornithine decarboxylase (ODC) / metal-dependent deubiquitinase activity / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome core complex / Somitogenesis / 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) / K63-linked deubiquitinase activity / Resolution of D-loop Structures through Holliday Junction Intermediates / transcription factor binding / proteasome binding / Impaired BRCA2 binding to RAD51 / regulation of protein catabolic process / myofibril / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / general transcription initiation factor binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / polyubiquitin modification-dependent protein binding / protein deubiquitination / blastocyst development / immune system process / proteasome endopeptidase complex / NF-kappaB binding / proteasome core complex, beta-subunit complex / endopeptidase activator activity / threonine-type endopeptidase activity / proteasome assembly / proteasome core complex, alpha-subunit complex / mRNA export from nucleus / enzyme regulator activity / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / ERAD pathway / regulation of proteasomal protein catabolic process / inclusion body / proteasome complex / TBP-class protein binding / : / Degradation of CDH1 / stem cell differentiation / sarcomere / Degradation of CRY and PER proteins / Regulation of activated PAK-2p34 by proteasome mediated degradation / 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 / negative regulation of inflammatory response to antigenic stimulus / Assembly of the pre-replicative complex / P-body / Vpu mediated degradation of CD4 / Degradation of DVL / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / lipopolysaccharide binding / Degradation of AXIN / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / G2/M Checkpoints / Hedgehog ligand biogenesis / Degradation of GLI1 by the proteasome / Defective CFTR causes cystic fibrosis / Autodegradation of the E3 ubiquitin ligase COP1 / Regulation of RUNX3 expression and activity / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Hedgehog 'on' state / Vif-mediated degradation of APOBEC3G / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / double-strand break repair via homologous recombination Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||
Authors | Huang XL / Luan B / Wu JP / Shi YG | ||||||||||||
| Funding support | China, 3 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2016Title: An atomic structure of the human 26S proteasome. Authors: Xiuliang Huang / Bai Luan / Jianping Wu / Yigong Shi / ![]() Abstract: We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory ...We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent α subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP α-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-Å resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function. | ||||||||||||
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Structure visualization
| Movie |
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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_9512.map.gz | 478.8 MB | EMDB map data format | |
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| Header (meta data) | emd-9512-v30.xml emd-9512.xml | 53.1 KB 53.1 KB | Display Display | EMDB header |
| Images | emd_9512.png | 32.5 KB | ||
| Filedesc metadata | emd-9512.cif.gz | 13.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-9512 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-9512 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5gjrMC ![]() 9507C ![]() 9508C ![]() 9509C ![]() 9510C ![]() 9511C ![]() 5gjqC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data |
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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_9512.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | with C2 symmetry | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 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 : human 26S proteasome
+Supramolecule #1: human 26S proteasome
+Macromolecule #1: 26S protease regulatory subunit 4
+Macromolecule #2: 26S protease regulatory subunit 7
+Macromolecule #3: 26S protease regulatory subunit 10B
+Macromolecule #4: 26S protease regulatory subunit 6A
+Macromolecule #5: 26S protease regulatory subunit 8
+Macromolecule #6: 26S protease regulatory subunit 6B
+Macromolecule #7: 26S proteasome non-ATPase regulatory subunit 1
+Macromolecule #8: 26S proteasome non-ATPase regulatory subunit 13
+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 3
+Macromolecule #13: 26S proteasome non-ATPase regulatory subunit 8
+Macromolecule #14: 26S proteasome non-ATPase regulatory subunit 7
+Macromolecule #15: 26S proteasome non-ATPase regulatory subunit 14
+Macromolecule #16: 26S proteasome non-ATPase regulatory subunit 4
+Macromolecule #17: 26S proteasome complex subunit DSS1
+Macromolecule #18: 26S proteasome non-ATPase regulatory subunit 2
+Macromolecule #19: Proteasome subunit alpha type-6
+Macromolecule #20: Proteasome subunit alpha type-2
+Macromolecule #21: Proteasome subunit alpha type-4
+Macromolecule #22: Proteasome subunit alpha type-7
+Macromolecule #23: Proteasome subunit alpha type-5
+Macromolecule #24: Proteasome subunit alpha type-1
+Macromolecule #25: Proteasome subunit alpha type-3
+Macromolecule #26: Proteasome subunit beta type-6
+Macromolecule #27: Proteasome subunit beta type-7
+Macromolecule #28: Proteasome subunit beta type-3
+Macromolecule #29: Proteasome subunit beta type-2
+Macromolecule #30: Proteasome subunit beta type-5
+Macromolecule #31: Proteasome subunit beta type-1
+Macromolecule #32: Proteasome subunit beta type-4
+Macromolecule #33: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL | ||||||||||||
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| Buffer | pH: 8 Component:
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| Grid | Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 3 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 2 seconds before plunging. | ||||||||||||
| Details | This sample was monodisperse. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Temperature | Min: 70.0 K |
| Details | Preliminary grid screening was performed manually |
| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Frames/image: 1-26 / Average exposure time: 1.6 sec. / Average electron dose: 37.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Calibrated defocus max: 0.0026000000000000003 µm / Calibrated defocus min: 0.0016 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


Keywords
Homo sapiens (human)
Authors
China, 3 items
Citation
UCSF Chimera






















Z (Sec.)
Y (Row.)
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