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- EMDB-2272: Cryo-EM structures of two intermediates provide insight into aden... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-2272 | |||||||||
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Title | Cryo-EM structures of two intermediates provide insight into adenovirus assembly and disassembly | |||||||||
![]() | Averaged hexon | |||||||||
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![]() | Adenovirus / intermediate | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
![]() | Cheng L / Huang X / Li X / Xiong W / Sun W / Yang C / Zhang K / Wang Y / Liu H / Ji G ...Cheng L / Huang X / Li X / Xiong W / Sun W / Yang C / Zhang K / Wang Y / Liu H / Ji G / Sun F / Zheng C / Zhu P | |||||||||
![]() | ![]() Title: Cryo-EM structures of two bovine adenovirus type 3 intermediates. Authors: Lingpeng Cheng / Xiaoxing Huang / Xiaomin Li / Wei Xiong / Wei Sun / Chongwen Yang / Kai Zhang / Ying Wang / Hongrong Liu / Xiaojun Huang / Gang Ji / Fei Sun / Congyi Zheng / Ping Zhu / ![]() Abstract: Adenoviruses (Ads) infect hosts from all vertebrate species and have been investigated as vaccine vectors. We report here near-atomic structures of two bovine Ad type 3 (BAd3) intermediates obtained ...Adenoviruses (Ads) infect hosts from all vertebrate species and have been investigated as vaccine vectors. We report here near-atomic structures of two bovine Ad type 3 (BAd3) intermediates obtained by cryo-electron microscopy. A comparison between the two intermediate structures reveals that the differences are localized in the fivefold vertex region, while their facet structures are identical. The overall facet structure of BAd3 exhibits a similar structure to human Ads; however, BAd3 protein IX has a unique conformation. Mass spectrometry and cryo-electron tomography analyses indicate that one intermediate structure represents the stage during DNA encapsidation, whilst the other intermediate structure represents a later stage. These results also suggest that cleavage of precursor protein VI occurs during, rather than after, the DNA encapsidation process. Overall, our results provide insights into the mechanism of Ad assembly, and allow the first structural comparison between human and nonhuman Ads at backbone level. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.8 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.2 KB 8.2 KB | Display Display | ![]() |
Images | ![]() | 297 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 329.9 KB | Display | ![]() |
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Full document | ![]() | 329 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Averaged hexon | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.16 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Disassembly and assembly intermediates of bovine adenovirus type 3
Entire | Name: Disassembly and assembly intermediates of bovine adenovirus type 3 |
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Components |
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-Supramolecule #1000: Disassembly and assembly intermediates of bovine adenovirus type 3
Supramolecule | Name: Disassembly and assembly intermediates of bovine adenovirus type 3 type: sample / ID: 1000 / Number unique components: 1 |
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-Supramolecule #1: Bovine adenovirus 3
Supramolecule | Name: Bovine adenovirus 3 / type: virus / ID: 1 / NCBI-ID: 10510 / Sci species name: Bovine adenovirus 3 / Database: NCBI / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK II |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Date | Jan 2, 2011 |
Image recording | Category: CCD / Film or detector model: GENERIC CCD / Average electron dose: 25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 125390 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 0.0035 µm / Nominal defocus min: 0.001 µm / Nominal magnification: 75000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Software - Name: ISAFs / Number images used: 28505 |
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