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Yorodumi- EMDB-42199: Eastern equine encephalitis virus (PE-6) VLP in complex with VLDL... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-42199 | |||||||||
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Title | Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-8)[W132A, W210A, W256A] (icosahedral) | |||||||||
Map data | EEEV PE-6 VLP in complex with VLDLR LA(1-8) W132A, W210A, W256A icosahedral reconstruction | |||||||||
Sample |
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Keywords | virus / receptor / VIRUS LIKE PARTICLE | |||||||||
Biological species | Eastern equine encephalitis virus | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.03 Å | |||||||||
Authors | Adams LJ / Fremont DH | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Cell / Year: 2024 Title: Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus. Authors: Lucas J Adams / Saravanan Raju / Hongming Ma / Theron Gilliland / Douglas S Reed / William B Klimstra / Daved H Fremont / Michael S Diamond / Abstract: The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and ...The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV). Here, by resolving multiple cryo-electron microscopy structures of EEEV-VLDLR complexes and performing mutagenesis and functional studies, we show that EEEV uses multiple sites (E1/E2 cleft and E2 A domain) to engage more than one LA domain simultaneously. However, no single LA domain is necessary or sufficient to support efficient EEEV infection. Whereas all EEEV strains show conservation of two VLDLR-binding sites, the EEEV PE-6 strain and a few other EEE complex members feature a single amino acid substitution that enables binding of LA domains to an additional site on the E2 B domain. These structural and functional analyses informed the design of a minimal VLDLR decoy receptor that neutralizes EEEV infection and protects mice from lethal challenge. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_42199.map.gz | 1.3 GB | EMDB map data format | |
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Header (meta data) | emd-42199-v30.xml emd-42199.xml | 14.2 KB 14.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_42199_fsc.xml | 25.2 KB | Display | FSC data file |
Images | emd_42199.png | 51 KB | ||
Filedesc metadata | emd-42199.cif.gz | 3.9 KB | ||
Others | emd_42199_additional_1.map.gz emd_42199_half_map_1.map.gz emd_42199_half_map_2.map.gz | 698.9 MB 1.3 GB 1.3 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42199 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42199 | HTTPS FTP |
-Validation report
Summary document | emd_42199_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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Full document | emd_42199_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | emd_42199_validation.xml.gz | 33.6 KB | Display | |
Data in CIF | emd_42199_validation.cif.gz | 45.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42199 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42199 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_42199.map.gz / Format: CCP4 / Size: 1.4 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-8) W132A, W210A, W256A icosahedral reconstruction | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.184 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: EEEV PE-6 VLP in complex with VLDLR LA(1-8)...
File | emd_42199_additional_1.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-8) W132A, W210A, W256A icosahedral reconstruction (unsharpened map) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: EEEV PE-6 VLP in complex with VLDLR LA(1-8)...
File | emd_42199_half_map_1.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-8) W132A, W210A, W256A icosahedral reconstruction (half map A) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: EEEV PE-6 VLP in complex with VLDLR LA(1-8)...
File | emd_42199_half_map_2.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-8) W132A, W210A, W256A icosahedral reconstruction (half map B) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Eastern equine encephalitis virus
Entire | Name: Eastern equine encephalitis virus |
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Components |
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-Supramolecule #1: Eastern equine encephalitis virus
Supramolecule | Name: Eastern equine encephalitis virus / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 11021 / Sci species name: Eastern equine encephalitis virus / Sci species strain: PE-6 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: Yes |
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-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 39.9 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: 1.9000000000000001 µm / Nominal defocus min: 0.5 µm |