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Yorodumi- EMDB-71741: Human 26S proteasome bound to TXNL1 with closed gate of core particle -
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Open data
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Basic information
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| Title | Human 26S proteasome bound to TXNL1 with closed gate of core particle | |||||||||
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Keywords | Proteasome / 26S / TXNL1 / HYDROLASE | |||||||||
| Function / homology | Function and homology informationdisulfide oxidoreductase activity / 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) / meiosis I / proteasome accessory complex / purine ribonucleoside triphosphate binding ...disulfide oxidoreductase activity / 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) / meiosis I / proteasome accessory complex / purine ribonucleoside triphosphate binding / integrator complex / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / Antigen processing: Ub, ATP-independent proteasomal degradation / RND1 GTPase cycle / RND2 GTPase cycle / RND3 GTPase cycle / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / RHOBTB1 GTPase cycle / sperm glycocalyx / protein K63-linked deubiquitination / RHOV GTPase cycle / negative regulation of programmed cell death / metal-dependent deubiquitinase activity / Regulation of ornithine decarboxylase (ODC) / perinuclear theca / proteasome core complex / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / transcription factor binding / K63-linked deubiquitinase activity / 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) / Resolution of D-loop Structures through Holliday Junction Intermediates / proteasome binding / RHOU GTPase cycle / Impaired BRCA2 binding to RAD51 / regulation of protein catabolic process / myofibril / protein-disulfide reductase activity / proteasome storage granule / sperm head-tail coupling apparatus / general transcription initiation factor binding / Presynaptic phase of homologous DNA pairing and strand exchange / blastocyst development / protein deubiquitination / immune system process / polyubiquitin modification-dependent protein binding / NF-kappaB binding / RHOBTB2 GTPase cycle / endopeptidase activator activity / proteasome core complex, alpha-subunit complex / mRNA export from nucleus / proteasome assembly / enzyme regulator activity / regulation of proteasomal protein catabolic process / inclusion body / : / TBP-class protein binding / proteasome complex / ciliary tip / stem cell differentiation / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / ubiquitin binding / Autodegradation of Cdh1 by Cdh1:APC/C / centriole / APC/C:Cdc20 mediated degradation of Securin / negative regulation of inflammatory response to antigenic stimulus / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / 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 / AUF1 (hnRNP D0) binds and destabilizes mRNA / sperm end piece / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / P-body / 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 Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
Authors | Chen X / Negi H / Walters KJ | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: To Be PublishedTitle: Structures of dynamic interactors at native proteasomes by PhIX-MS and cryo-electron microscopy Authors: Lee K / Negi H / Chen X / Atallah-Yunes K / Truslow S / Castelino RE / Guest M / Ciancone AM / Lu X / Tarasov SG / Chari R / Walters KJ / O'Reilly FJ | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_71741.map.gz | 203.5 MB | EMDB map data format | |
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| Header (meta data) | emd-71741-v30.xml emd-71741.xml | 68.5 KB 68.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_71741_fsc.xml | 15.9 KB | Display | FSC data file |
| Images | emd_71741.png | 73.8 KB | ||
| Filedesc metadata | emd-71741.cif.gz | 14.9 KB | ||
| Others | emd_71741_additional_1.map.gz emd_71741_half_map_1.map.gz emd_71741_half_map_2.map.gz | 275.5 MB 391 MB 391 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-71741 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-71741 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9pmqMC ![]() 12bmC ![]() 9pmjC ![]() 9pmoC ![]() 9proC ![]() 9prtC 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_71741.map.gz / Format: CCP4 / Size: 421.9 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: 0.81 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_71741_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_71741_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_71741_half_map_2.map | ||||||||||||
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Sample components
+Entire : Human proteasome from HCT116 cells
+Supramolecule #1: Human proteasome from HCT116 cells
+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: 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: Isoform Long of Proteasome subunit alpha type-1
+Macromolecule #13: Proteasome subunit alpha type-3
+Macromolecule #14: 26S proteasome non-ATPase regulatory subunit 1
+Macromolecule #15: 26S proteasome non-ATPase regulatory subunit 3
+Macromolecule #16: 26S proteasome non-ATPase regulatory subunit 12
+Macromolecule #17: 26S proteasome non-ATPase regulatory subunit 11
+Macromolecule #18: 26S proteasome non-ATPase regulatory subunit 6
+Macromolecule #19: 26S proteasome non-ATPase regulatory subunit 7
+Macromolecule #20: 26S proteasome non-ATPase regulatory subunit 13
+Macromolecule #21: 26S proteasome non-ATPase regulatory subunit 4
+Macromolecule #22: 26S proteasome non-ATPase regulatory subunit 14
+Macromolecule #23: 26S proteasome non-ATPase regulatory subunit 8
+Macromolecule #24: 26S proteasome complex subunit SEM1
+Macromolecule #25: 26S proteasome non-ATPase regulatory subunit 2
+Macromolecule #26: Thioredoxin-like protein 1
+Macromolecule #27: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
+Macromolecule #28: MAGNESIUM ION
+Macromolecule #29: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #30: 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
| Concentration | 0.75 mg/mL | ||||||||||||||||||
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| Buffer | pH: 7.5 Component:
Details: 50 mM Tris [pH7.5], 50 mM NaCl, 1.5 mM ATP-gamma-S, 5 mM MgCl2 and 2 mM DTT | ||||||||||||||||||
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Details: 25 mA | ||||||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 295.15 K / Instrument: LEICA EM GP | ||||||||||||||||||
| Details | Quantifoil copper R 1.2/1.3 holey carbon 300 mesh grids (#Q3100CR1.3; Electron Microscopy Sciences). |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Specialist optics | Energy filter - Name: GIF Bioquantum |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number real images: 40 / Average exposure time: 2.5 sec. / Average electron dose: 55.6 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 100000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model |
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| Refinement | Space: REAL / Protocol: RIGID BODY FIT / Overall B value: 41.8 / Target criteria: Cross-correlation coefficient | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Output model | ![]() PDB-9pmq: |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States, 1 items
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Z (Sec.)
Y (Row.)
X (Col.)














































FIELD EMISSION GUN



