+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-2047 | |||||||||
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Title | Structure of the human 26S proteasome | |||||||||
Map data | The deposited map has been supersampled to a grid of 1.412 angstroms (from the experimental 2.824 angstroms) for improved display | |||||||||
Sample |
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Keywords | 26S proteasome / proteasome / 20S / 19S / human | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.0 Å | |||||||||
Authors | da Fonseca PCA / He J / Morris EP | |||||||||
Citation | Journal: Mol Cell / Year: 2012 Title: Molecular model of the human 26S proteasome. Authors: Paula C A da Fonseca / Jun He / Edward P Morris / Abstract: The 26S proteasome plays a fundamental role in eukaryotic homeostasis by undertaking the highly controlled degradation of a wide range of proteins, including key cellular regulators such as those ...The 26S proteasome plays a fundamental role in eukaryotic homeostasis by undertaking the highly controlled degradation of a wide range of proteins, including key cellular regulators such as those controlling cell-cycle progression and apoptosis. Here we report the structure of the human 26S proteasome determined by cryo-electron microscopy and single-particle analysis, with secondary structure elements identified both in the 20S proteolytic core region and in the 19S regulatory particle. We have used this information together with crystal structures, homology models, and other biochemical information to construct a molecular model of the complete 26S proteasome. This model allows for a detailed description of the 20S core within the 26S proteasome and redefines the overall assignment of subunits within the 19S regulatory particle. The information presented here provides a strong basis for a mechanistic understanding of the 26S proteasome. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_2047.map.gz | 34.5 MB | EMDB map data format | |
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Header (meta data) | emd-2047-v30.xml emd-2047.xml | 7.8 KB 7.8 KB | Display Display | EMDB header |
Images | EMDEP_2047.jpg | 59.1 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-2047 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-2047 | HTTPS FTP |
-Validation report
Summary document | emd_2047_validation.pdf.gz | 203.9 KB | Display | EMDB validaton report |
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Full document | emd_2047_full_validation.pdf.gz | 203 KB | Display | |
Data in XML | emd_2047_validation.xml.gz | 4.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-2047 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-2047 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_2047.map.gz / Format: CCP4 / Size: 42.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | The deposited map has been supersampled to a grid of 1.412 angstroms (from the experimental 2.824 angstroms) for improved display | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.412 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : 26S proteasome
Entire | Name: 26S proteasome |
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Components |
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-Supramolecule #1000: 26S proteasome
Supramolecule | Name: 26S proteasome / type: sample / ID: 1000 / Oligomeric state: dimer / Number unique components: 1 |
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Molecular weight | Theoretical: 2.6 MDa |
-Macromolecule #1: 26S proteasome
Macromolecule | Name: 26S proteasome / type: protein_or_peptide / ID: 1 / Oligomeric state: dimer / Recombinant expression: No |
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Source (natural) | Organism: Homo sapiens (human) / synonym: Human / Cell: Erythrocyte |
Molecular weight | Theoretical: 2.6 MDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.15 mg/mL |
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Buffer | Details: 50 mM Tris-HCl, pH 7.5, mM MgCl2, 2 mM ATP and 1 mM dithiotreitol |
Grid | Details: Quantifoil coated with thin layer of carbon |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Instrument: FEI VITROBOT MARK III / Method: Blot for 5 seconds |
-Electron microscopy
Microscope | FEI TECNAI F20 |
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Details | CCD images binned x2 |
Date | Oct 20, 2010 |
Image recording | Category: CCD / Film or detector model: TVIPS TEMCAM-F415 (4k x 4k) / Average electron dose: 25 e/Å2 / Bits/pixel: 16 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.475 µm / Nominal defocus min: 1.1 µm / Nominal magnification: 63000 |
Sample stage | Specimen holder model: GATAN LIQUID NITROGEN |
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |
-Image processing
CTF correction | Details: CCD frame |
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Final reconstruction | Applied symmetry - Point group: C2 (2 fold cyclic) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 7.0 Å / Resolution method: OTHER / Software - Name: IMAGIC,Spider,in-house,software / Number images used: 12718 |