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Yorodumi- EMDB-31292: Human Cytomegalovirus, the reconstruction of C1 capsid in the env... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31292 | |||||||||
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Title | Human Cytomegalovirus, the reconstruction of C1 capsid in the enveloped capsid | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information T=16 icosahedral viral capsid / viral genome packaging / viral tegument / viral capsid assembly / viral release from host cell / chromosome organization / viral process / virion component / viral capsid / symbiont-mediated perturbation of host ubiquitin-like protein modification ...T=16 icosahedral viral capsid / viral genome packaging / viral tegument / viral capsid assembly / viral release from host cell / chromosome organization / viral process / virion component / viral capsid / symbiont-mediated perturbation of host ubiquitin-like protein modification / host cell cytoplasm / cysteine-type deubiquitinase activity / host cell nucleus / structural molecule activity / proteolysis / DNA binding Similarity search - Function | |||||||||
Biological species | Human betaherpesvirus 5 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.8 Å | |||||||||
Authors | Li Z / Pang J / Dong L / Yu X | |||||||||
Funding support | China, 1 items
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Citation | Journal: Nat Commun / Year: 2021 Title: Structural basis for genome packaging, retention, and ejection in human cytomegalovirus. Authors: Zhihai Li / Jingjing Pang / Lili Dong / Xuekui Yu / Abstract: How the human cytomegalovirus (HCMV) genome-the largest among human herpesviruses-is packaged, retained, and ejected remains unclear. We present the in situ structures of the symmetry-mismatched ...How the human cytomegalovirus (HCMV) genome-the largest among human herpesviruses-is packaged, retained, and ejected remains unclear. We present the in situ structures of the symmetry-mismatched portal and the capsid vertex-specific components (CVSCs) of HCMV. The 5-fold symmetric 10-helix anchor-uncommon among known portals-contacts the portal-encircling DNA, which is presumed to squeeze the portal as the genome packaging proceeds. We surmise that the 10-helix anchor dampens this action to delay the portal reaching a "head-full" packaging state, thus facilitating the large genome to be packaged. The 6-fold symmetric turret, latched via a coiled coil to a helix from a major capsid protein, supports the portal to retain the packaged genome. CVSCs at the penton vertices-presumed to increase inner capsid pressure-display a low stoichiometry, which would aid genome retention. We also demonstrate that the portal and capsid undergo conformational changes to facilitate genome ejection after viral cell entry. | |||||||||
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_31292.map.gz | 467.4 MB | EMDB map data format | |
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Header (meta data) | emd-31292-v30.xml emd-31292.xml | 7.4 KB 7.4 KB | Display Display | EMDB header |
Images | emd_31292.png | 34.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31292 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31292 | HTTPS FTP |
-Validation report
Summary document | emd_31292_validation.pdf.gz | 412.6 KB | Display | EMDB validaton report |
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Full document | emd_31292_full_validation.pdf.gz | 412.1 KB | Display | |
Data in XML | emd_31292_validation.xml.gz | 7.5 KB | Display | |
Data in CIF | emd_31292_validation.cif.gz | 8.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31292 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31292 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_31292.map.gz / Format: CCP4 / Size: 512 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: 3.25 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 : Human betaherpesvirus 5
Entire | Name: Human betaherpesvirus 5 |
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Components |
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-Supramolecule #1: Human betaherpesvirus 5
Supramolecule | Name: Human betaherpesvirus 5 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10359 / Sci species name: Human betaherpesvirus 5 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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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: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 22087 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |