+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20083 | |||||||||
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Title | Cryo-EM reconstruction of Sulfolobus polyhedral virus 1 (SPV1) | |||||||||
Map data | Cryo-EM reconstruction of Sulfolobus polyhedral virus 1 (SPV1) | |||||||||
Sample |
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Keywords | archaeal pilus / STRUCTURAL PROTEIN / icosahedral symmetry / VIRUS | |||||||||
Function / homology | icosahedral viral capsid / Capsid protein VP10 / Capsid protein VP4 Function and homology information | |||||||||
Biological species | Sulfolobus polyhedral virus 1 / Sulfolobus spindle-shaped virus 1 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Wang F / Liu Y | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2019 Title: A packing for A-form DNA in an icosahedral virus. Authors: Fengbin Wang / Ying Liu / Zhangli Su / Tomasz Osinski / Guilherme A P de Oliveira / James F Conway / Stefan Schouten / Mart Krupovic / David Prangishvili / Edward H Egelman / Abstract: Studies on viruses infecting archaea living in the most extreme environments continue to show a remarkable diversity of structures, suggesting that the sampling continues to be very sparse. We have ...Studies on viruses infecting archaea living in the most extreme environments continue to show a remarkable diversity of structures, suggesting that the sampling continues to be very sparse. We have used electron cryo-microscopy to study at 3.7-Å resolution the structure of the polyhedral virus 1 (SPV1), which was originally isolated from a hot, acidic spring in Beppu, Japan. The 2 capsid proteins with variant single jelly-roll folds form pentamers and hexamers which assemble into a = 43 icosahedral shell. In contrast to tailed icosahedral double-stranded DNA (dsDNA) viruses infecting bacteria and archaea, and herpesviruses infecting animals and humans, where naked DNA is packed under very high pressure due to the repulsion between adjacent layers of DNA, the circular dsDNA in SPV1 is fully covered with a viral protein forming a nucleoprotein filament with attractive interactions between layers. Most strikingly, we have been able to show that the DNA is in an A-form, as it is in the filamentous viruses infecting hyperthermophilic acidophiles. Previous studies have suggested that DNA is in the B-form in bacteriophages, and our study is a direct visualization of the structure of DNA in an icosahedral virus. | |||||||||
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_20083.map.gz | 1.7 GB | EMDB map data format | |
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Header (meta data) | emd-20083-v30.xml emd-20083.xml | 10.9 KB 10.9 KB | Display Display | EMDB header |
Images | emd_20083.png | 248.8 KB | ||
Filedesc metadata | emd-20083.cif.gz | 5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20083 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20083 | HTTPS FTP |
-Validation report
Summary document | emd_20083_validation.pdf.gz | 748.2 KB | Display | EMDB validaton report |
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Full document | emd_20083_full_validation.pdf.gz | 747.7 KB | Display | |
Data in XML | emd_20083_validation.xml.gz | 9.4 KB | Display | |
Data in CIF | emd_20083_validation.cif.gz | 10.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20083 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20083 | HTTPS FTP |
-Related structure data
Related structure data | 6oj0MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_20083.map.gz / Format: CCP4 / Size: 1.9 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Cryo-EM reconstruction of Sulfolobus polyhedral virus 1 (SPV1) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.4 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 : Sulfolobus spindle-shaped virus 1
Entire | Name: Sulfolobus spindle-shaped virus 1 |
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Components |
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-Supramolecule #1: Sulfolobus spindle-shaped virus 1
Supramolecule | Name: Sulfolobus spindle-shaped virus 1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 244589 / Sci species name: Sulfolobus spindle-shaped virus 1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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Host (natural) | Organism: Sulfolobus sp. S38A |
-Macromolecule #1: Structural protein VP4
Macromolecule | Name: Structural protein VP4 / type: protein_or_peptide / ID: 1 / Number of copies: 42 / Enantiomer: LEVO |
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Source (natural) | Organism: Sulfolobus polyhedral virus 1 |
Molecular weight | Theoretical: 19.394885 KDa |
Sequence | String: MSESVTQQVF NFAVTKSQPF GGYVYSTNLT ASTSSAVTST QLTPLNLSIT LGQITLSGNS LVIPATQIWY LTDAYVSVPD YTNITNGAE ADGVILIYKD GVKLMLTTPL ISSMSISNPA RTHLAQAVKY SPQSILTMYF NPTKPATAST SYPNTVYFTV V VVDFSYAQ NPARAVVSAN AVM UniProtKB: Capsid protein VP4 |
-Macromolecule #2: Uncharacterized protein
Macromolecule | Name: Uncharacterized protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Sulfolobus polyhedral virus 1 |
Molecular weight | Theoretical: 20.617277 KDa |
Sequence | String: MLSLDNYSYV HNITTQTNID LSSQQTIHLA SINGKGYIIF LRFFCEGSSA CFTNVKFSVK ANGLVLYSFR YIQLLELGQA IATAIPSSS QGFSTLLSNY NVLISSPIGT LPQLTLYDSY DNRYGAMLQP AFPLPFVNTL SLDVDILPVS QSSYDPIPYS L NDNQISTN APTGKGNISI EYLLYNCLV UniProtKB: Capsid protein VP10 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 4 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 20.0 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
Startup model | Type of model: OTHER / Details: sphere |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: OTHER / Software - Name: RELION / Details: d99, model:map FSC (0.38), map:map FSC (0.143) / Number images used: 19092 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |