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Open data
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Basic information
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Title | AcMNPV apical cap - C14 anchor complex only | |||||||||
![]() | AcMNPV apical cap - C14 anchor complex only | |||||||||
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![]() | nucleocapsid / VIRUS | |||||||||
Function / homology | ![]() transport of viral material towards nucleus / exit of virus from host cell nucleus by nuclear egress / host cell nuclear matrix / symbiont-mediated perturbation of host cell cycle progression / nuclear capsid assembly / polynucleotide 5'-phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity, metal-dependent / histone H2AXY142 phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity ...transport of viral material towards nucleus / exit of virus from host cell nucleus by nuclear egress / host cell nuclear matrix / symbiont-mediated perturbation of host cell cycle progression / nuclear capsid assembly / polynucleotide 5'-phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity, metal-dependent / histone H2AXY142 phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity / virion component / viral capsid / host cell / viral nucleocapsid / host cell cytoplasm / viral envelope / host cell nucleus / virion membrane / structural molecule activity / protein homodimerization activity / DNA binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.7 Å | |||||||||
![]() | Effantin G / Kandiah E / Pelosse M | |||||||||
Funding support | 1 items
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![]() | ![]() Title: 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
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Downloads & links
-EMDB archive
Map data | ![]() | 379.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.3 KB 24.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.7 KB | Display | ![]() |
Images | ![]() | 91.4 KB | ||
Masks | ![]() | 476.8 MB | ![]() | |
Filedesc metadata | ![]() | 7.9 KB | ||
Others | ![]() ![]() | 379.5 MB 379.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9h2jMC ![]() 9h1sC ![]() 9h2aC ![]() 9h2bC ![]() 9h2cC ![]() 9h2hC ![]() 9h2kC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | AcMNPV apical cap - C14 anchor complex only | ||||||||||||||||||||||||||||||||||||
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
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Density Histograms |
-Half map: AcMNPV apical cap - C14 anchor complex only - half map 1
File | emd_51808_half_map_1.map | ||||||||||||
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Annotation | AcMNPV apical cap - C14 anchor complex only - half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: AcMNPV apical cap - C14 anchor complex only - half map 2
File | emd_51808_half_map_2.map | ||||||||||||
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Annotation | AcMNPV apical cap - C14 anchor complex only - half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Autographa californica nucleopolyhedrovirus
+Supramolecule #1: Autographa californica nucleopolyhedrovirus
+Macromolecule #1: Occlusion-derived virus envelope protein E27
+Macromolecule #2: Protein C42
+Macromolecule #3: Protein AC142
+Macromolecule #4: Major capsid protein
+Macromolecule #5: Capsid-associated protein VP80
+Macromolecule #6: Protein AC109
+Macromolecule #7: Protein Ac66
+Macromolecule #8: Tyrosine-protein phosphatase
+Macromolecule #9: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | 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: ![]() |
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 |