+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-47021 | |||||||||
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Title | Glycosylated chronic wasting disease prion fibril | |||||||||
Map data | CWD density modified real-space symmetrized map | |||||||||
Sample |
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Keywords | Prion / Chronic Wasting Disease / Deer / Fibril / GPI-anchor / Glycosylation / PrP / Infectious / Amyloid / Brain-derived / ex vivo / Prion strain / PROTEIN FIBRIL | |||||||||
Function / homology | Function and homology information side of membrane / protein homooligomerization / Golgi apparatus / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Odocoileus virginianus (white-tailed deer) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Caughey B / Hoyt F / Alam P / Artikis E / Soukup J / Hughson A / Schwartz C / Race B / Barbian K | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Acta Neuropathol / Year: 2024 Title: Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer. Authors: Parvez Alam / Forrest Hoyt / Efrosini Artikis / Jakub Soukup / Andrew G Hughson / Cindi L Schwartz / Kent Barbian / Michael W Miller / Brent Race / Byron Caughey / Abstract: Chronic wasting disease (CWD) is a widely distributed prion disease of cervids with implications for wildlife conservation and also for human and livestock health. The structures of infectious prions ...Chronic wasting disease (CWD) is a widely distributed prion disease of cervids with implications for wildlife conservation and also for human and livestock health. The structures of infectious prions that cause CWD and other natural prion diseases of mammalian hosts have been poorly understood. Here we report a 2.8 Å resolution cryogenic electron microscopy-based structure of CWD prion fibrils from the brain of a naturally infected white-tailed deer expressing the most common wild-type PrP sequence. Like recently solved rodent-adapted scrapie prion fibrils, our atomic model of CWD fibrils contains single stacks of PrP molecules forming parallel in-register intermolecular β-sheets and intervening loops comprising major N- and C-terminal lobes within the fibril cross-section. However, CWD fibrils from a natural cervid host differ markedly from the rodent structures in many other features, including a ~ 180° twist in the relative orientation of the lobes. This CWD structure suggests mechanisms underlying the apparent CWD transmission barrier to humans and should facilitate more rational approaches to the development of CWD vaccines and therapeutics. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_47021.map.gz | 42.4 MB | EMDB map data format | |
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Header (meta data) | emd-47021-v30.xml emd-47021.xml | 16.5 KB 16.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_47021_fsc.xml | 13.6 KB | Display | FSC data file |
Images | emd_47021.png | 80.1 KB | ||
Masks | emd_47021_msk_1.map | 216 MB | Mask map | |
Filedesc metadata | emd-47021.cif.gz | 5.9 KB | ||
Others | emd_47021_half_map_1.map.gz emd_47021_half_map_2.map.gz | 171.8 MB 171.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-47021 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-47021 | HTTPS FTP |
-Validation report
Summary document | emd_47021_validation.pdf.gz | 1012.8 KB | Display | EMDB validaton report |
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Full document | emd_47021_full_validation.pdf.gz | 1012.3 KB | Display | |
Data in XML | emd_47021_validation.xml.gz | 21.8 KB | Display | |
Data in CIF | emd_47021_validation.cif.gz | 28.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47021 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47021 | HTTPS FTP |
-Related structure data
Related structure data | 9dmzMC 9dmyC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_47021.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | CWD density modified real-space symmetrized map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8284 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_47021_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_47021_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_47021_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Naturally occurring chronic wasting disease prion fibril
Entire | Name: Naturally occurring chronic wasting disease prion fibril |
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Components |
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-Supramolecule #1: Naturally occurring chronic wasting disease prion fibril
Supramolecule | Name: Naturally occurring chronic wasting disease prion fibril type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Odocoileus virginianus (white-tailed deer) / Organ: Brain |
-Macromolecule #1: Major prion protein
Macromolecule | Name: Major prion protein / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Odocoileus virginianus (white-tailed deer) |
Molecular weight | Theoretical: 27.965486 KDa |
Sequence | String: MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW GQPHGGGWGQ PHGGGWGQPH GGGWGQPHG GGGWGQGGTH SQWNKPSKPK TNMKHVAGAA AAGAVVGGLG GYMLGSAMSR PLIHFGNDYE DRYYRENMYR Y PNQVYYRP ...String: MVKSHIGSWI LVLFVAMWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW GQPHGGGWGQ PHGGGWGQPH GGGWGQPHG GGGWGQGGTH SQWNKPSKPK TNMKHVAGAA AAGAVVGGLG GYMLGSAMSR PLIHFGNDYE DRYYRENMYR Y PNQVYYRP VDQYNNQNTF VHDCVNITVK QHTVTTTTKG ENFTETDIKM MERVVEQMCI TQYQRESQAY YQRGASVILF SS PPVILLI SFLIFLIVG UniProtKB: Major prion protein |
-Macromolecule #2: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 2 / Number of copies: 10 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 295 K / Instrument: LEICA EM GP |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | PDB-9dmz: |