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Yorodumi- EMDB-72428: Icosahedral symmetric structure of an expansion intermediate of T... -
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Basic information
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| Title | Icosahedral symmetric structure of an expansion intermediate of Turnip Crinkle Virus (Asymmetric Trimer Unit) | |||||||||
Map data | Icosahedral symmetry averaged structure of an expansion intermediate of Turnip Crinkle Virus | |||||||||
Sample |
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Keywords | Icosahedral non-enveloped ssRNA virus / Expansion intermediate / VIRUS | |||||||||
| Function / homology | Plant viruses icosahedral capsid proteins 'S' region signature. / Icosahedral viral capsid protein, S domain / Viral coat protein (S domain) / T=3 icosahedral viral capsid / Viral coat protein subunit / symbiont-mediated suppression of host innate immune response / structural molecule activity / RNA binding / Capsid protein Function and homology information | |||||||||
| Biological species | Turnip crinkle virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.87 Å | |||||||||
Authors | Venkatakrishnan V / Braet S / Ramesh R / Clawson MA / Laremore TN / Wong SM / Anand GS | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Sci Adv / Year: 2025Title: Asymmetric isopeptide bond steers directional genomic RNA egress from icosahedral virus. Authors: Sean M Braet / Varun Venkatakrishnan / Ranita Ramesh / Molly A Clawson / Tatiana N Laremore / Sek-Man Wong / Ganesh S Anand / ![]() Abstract: Icosahedral RNA viruses rely upon essential asymmetries for directional genome egress into the host cell. How these asymmetric egress points are built into the quaternary assembly of the virion is ...Icosahedral RNA viruses rely upon essential asymmetries for directional genome egress into the host cell. How these asymmetric egress points are built into the quaternary assembly of the virion is unknown. Here, we capture the structure and dynamics of a partially expanded virus disassembly intermediate, poised to release its spring-loaded genomic RNA. The structure shows highly localized density of RNA underneath surface fivefold axes on one-half of the viral particle. This polarity in RNA distribution is associated with a unique interchain isopeptide bond (glutamic acid-lysine), which flanks conserved high-affinity RNA binding sites. This singular isopeptide bond at the asymmetric egress site confers an essential "loaded-die" feature that is critical for steering genomic RNA egress into the host cell for virus propagation. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_72428.map.gz | 777.2 MB | EMDB map data format | |
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| Header (meta data) | emd-72428-v30.xml emd-72428.xml | 21.4 KB 21.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_72428_fsc.xml | 19.7 KB | Display | FSC data file |
| Images | emd_72428.png | 117 KB | ||
| Filedesc metadata | emd-72428.cif.gz | 6.5 KB | ||
| Others | emd_72428_half_map_1.map.gz emd_72428_half_map_2.map.gz | 761.8 MB 761.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72428 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72428 | HTTPS FTP |
-Validation report
| Summary document | emd_72428_validation.pdf.gz | 966.1 KB | Display | EMDB validaton report |
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| Full document | emd_72428_full_validation.pdf.gz | 965.6 KB | Display | |
| Data in XML | emd_72428_validation.xml.gz | 30 KB | Display | |
| Data in CIF | emd_72428_validation.cif.gz | 39.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-72428 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-72428 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9y2zMC ![]() 9y31C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_72428.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Icosahedral symmetry averaged structure of an expansion intermediate of Turnip Crinkle Virus | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.0644 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Icosahedral symmetry averaged hap map of an expansion...
| File | emd_72428_half_map_1.map | ||||||||||||
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| Annotation | Icosahedral symmetry averaged hap map of an expansion intermediate of Turnip Crinkle Virus | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Icosahedral symmetry averaged hap map of an expansion...
| File | emd_72428_half_map_2.map | ||||||||||||
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| Annotation | Icosahedral symmetry averaged hap map of an expansion intermediate of Turnip Crinkle Virus | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Turnip crinkle virus
| Entire | Name: Turnip crinkle virus |
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| Components |
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-Supramolecule #1: Turnip crinkle virus
| Supramolecule | Name: Turnip crinkle virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 11988 / Sci species name: Turnip crinkle virus / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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| Host (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 8.2 MDa |
| Virus shell | Shell ID: 1 / Diameter: 350.0 Å / T number (triangulation number): 3 |
-Macromolecule #1: Capsid protein
| Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 1 / Details: TCV CP / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Turnip crinkle virus |
| Molecular weight | Theoretical: 38.170941 KDa |
| Sequence | String: MENDPRVRKF ASDGAQWAIK WQKKGWSTLT SRQKQTARAA MGIKLSPVAQ PVQKVTRLSA PVALAYREVS TQPRVSTARD GITRSGSEL ITTLKKNTDT EPKYTTAVLN PSEPGTFNQL IKEAAQYEKY RFTSLRFRYS PMSPSTTGGK VALAFDRDAA K PPPNDLAS ...String: MENDPRVRKF ASDGAQWAIK WQKKGWSTLT SRQKQTARAA MGIKLSPVAQ PVQKVTRLSA PVALAYREVS TQPRVSTARD GITRSGSEL ITTLKKNTDT EPKYTTAVLN PSEPGTFNQL IKEAAQYEKY RFTSLRFRYS PMSPSTTGGK VALAFDRDAA K PPPNDLAS LYNIEGCVSS VPWTGFILTV PTDSTDRFVA DGISDPKLVD FGKLIMATYG QGANDAAQLG EVRVEYTVQL KN RTGSTSD AQIGDFAGVK DGPRLVSWSK TKGTAGWEHD CHFLGTGNFS LTLFYEKAPV SGLENADASD FSVLGEAAAG SVQ WAGVKV AERGQGVKMV TTEEQPKGKW QALRI UniProtKB: Capsid protein |
-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: 5.4 / Component - Concentration: 20.0 mM / Component - Formula: CH3COONa / Component - Name: Sodium Acetate |
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| Grid | Model: Quantifoil R2/2 / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Number real images: 2036 / Average electron dose: 25.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 40.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
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| Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 76 |
| Output model | ![]() PDB-9y2z: |
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About Yorodumi



Turnip crinkle virus
Keywords
Authors
United States, 1 items
Citation





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FIELD EMISSION GUN


