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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | AcMNPV apical cap - C2 plug only -consensus 3D map | |||||||||
Map data | AcMNPV apical cap - C2 plug consensus map | |||||||||
Sample |
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Keywords | nucleocapsid / VIRUS | |||||||||
| Biological species | Autographa californica nucleopolyhedrovirus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.6 Å | |||||||||
Authors | Effantin G / Kandiah E / Pelosse M | |||||||||
| Funding support | 1 items
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Citation | Journal: Nat Commun / Year: 2025Title: Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus. Authors: Gregory Effantin / Eaazhisai Kandiah / Martin Pelosse / ![]() Abstract: Baculoviruses are large DNA viruses found in nature propagating amongst insects and lepidoptera in particular. They have been studied for decades and are nowadays considered as invaluable ...Baculoviruses are large DNA viruses found in nature propagating amongst insects and lepidoptera in particular. They have been studied for decades and are nowadays considered as invaluable biotechnology tools used as biopesticides, recombinant expression systems or delivery vehicle for gene therapy. However, little is known about the baculovirus nucleocapsid assembly at a molecular level. Here, we solve the whole structure of the Autographa californica multiple nucleopolyhedrovirus (AcMNPV) nucleocapsid by applying cryo-electron microscopy (CryoEM) combined with de novo modelling and Alphafold predictions. Our structure completes prior observations and elucidates the intricate architecture of the apical cap, unravelling the organization of a DNA portal featuring intriguing symmetry mismatches between its core and vertex. The core, closing the capsid at the apex, holds two DNA helices of the viral genome tethered to Ac54 proteins. Different symmetry components at the apical cap and basal structure are constituted of the same building block, made of Ac101/Ac144, proving the versatility of this modular pair. The crown forming the portal vertex displays a C21 symmetry and contains, amongst others, the motor-like protein Ac66. Our findings support the viral portal to be involved in DNA packaging, probably in conjunction with other parts of a larger DNA packaging apparatus. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51805.map.gz | 79.3 MB | EMDB map data format | |
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| Header (meta data) | emd-51805-v30.xml emd-51805.xml | 14.2 KB 14.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51805_fsc.xml | 10.7 KB | Display | FSC data file |
| Images | emd_51805.png | 47.3 KB | ||
| Masks | emd_51805_msk_1.map | 103 MB | Mask map | |
| Filedesc metadata | emd-51805.cif.gz | 3.8 KB | ||
| Others | emd_51805_half_map_1.map.gz emd_51805_half_map_2.map.gz | 79.4 MB 79.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51805 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51805 | HTTPS FTP |
-Validation report
| Summary document | emd_51805_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_51805_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_51805_validation.xml.gz | 17.7 KB | Display | |
| Data in CIF | emd_51805_validation.cif.gz | 23.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51805 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51805 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_51805.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | AcMNPV apical cap - C2 plug consensus map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.35 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51805_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: AcMNPV apical cap - C2 plug consensus map - half map 1
| File | emd_51805_half_map_1.map | ||||||||||||
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| Annotation | AcMNPV apical cap - C2 plug consensus map - half map 1 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: AcMNPV apical cap - C2 plug consensus map - half map 2
| File | emd_51805_half_map_2.map | ||||||||||||
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| Annotation | AcMNPV apical cap - C2 plug consensus map - half map 2 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Autographa californica nucleopolyhedrovirus
| Entire | Name: Autographa californica nucleopolyhedrovirus |
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| Components |
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-Supramolecule #1: Autographa californica nucleopolyhedrovirus
| Supramolecule | Name: Autographa californica nucleopolyhedrovirus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#15 / NCBI-ID: 46015 Sci species name: Autographa californica nucleopolyhedrovirus 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 |
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Sample preparation
| Buffer | pH: 7 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS 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 / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Autographa californica nucleopolyhedrovirus
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Processing
FIELD EMISSION GUN

