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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Human 20S core particle beta7 tagged | |||||||||
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Sample |
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Keywords | Complex / HYDROLASE | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.22 Å | |||||||||
Authors | Schulman BA / Hanna JW / Harper JW / Adolf F / Du J / Rawson SD / Walsh Jr RM / Goodall EA | |||||||||
| Funding support | Germany, United States, 2 items
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Citation | Journal: bioRxiv / Year: 2024 Title: Visualizing chaperone-mediated multistep assembly of the human 20S proteasome. Authors: Frank Adolf / Jiale Du / Ellen A Goodall / Richard M Walsh / Shaun Rawson / Susanne von Gronau / J Wade Harper / John Hanna / Brenda A Schulman / ![]() Abstract: Dedicated assembly factors orchestrate stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here, we report cryo- ...Dedicated assembly factors orchestrate stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here, we report cryo-EM reconstructions of seven recombinant human subcomplexes that visualize all five chaperones and the three active site propeptides across a wide swath of the assembly pathway. Comparison of these chaperone-bound intermediates and a matching mature CP reveals molecular mechanisms determining the order of successive subunit additions, and how proteasome subcomplexes and assembly factors structurally adapt upon progressive subunit incorporation to stabilize intermediates, facilitate the formation of subsequent intermediates, and ultimately rearrange to coordinate proteolytic activation with gated access to active sites. The structural findings reported here explain many previous biochemical and genetic observations. This work establishes a methodologic approach for structural analysis of multiprotein complex assembly intermediates, illuminates specific functions of assembly factors, and reveals conceptual principles underlying human proteasome biogenesis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_19343.map.gz | 43.4 MB | EMDB map data format | |
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| Header (meta data) | emd-19343-v30.xml emd-19343.xml | 13.5 KB 13.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_19343_fsc.xml | 9.2 KB | Display | FSC data file |
| Images | emd_19343.png | 854.3 KB | ||
| Masks | emd_19343_msk_1.map | 83.7 MB | Mask map | |
| Filedesc metadata | emd-19343.cif.gz | 4 KB | ||
| Others | emd_19343_half_map_1.map.gz emd_19343_half_map_2.map.gz | 77.5 MB 77.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19343 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19343 | HTTPS FTP |
-Validation report
| Summary document | emd_19343_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_19343_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_19343_validation.xml.gz | 17.4 KB | Display | |
| Data in CIF | emd_19343_validation.cif.gz | 21.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19343 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19343 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_19343.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_19343_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_19343_half_map_1.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Human 20S core particle beta7 tagged
| Entire | Name: Human 20S core particle beta7 tagged |
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| Components |
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-Supramolecule #1: Human 20S core particle beta7 tagged
| Supramolecule | Name: Human 20S core particle beta7 tagged / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: Homo sapiens (human) |
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.0 µm |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Germany,
United States, 2 items
Citation















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Processing
FIELD EMISSION GUN
