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- PDB-8roq: FAdV-C4 Aviadenovirus structure, strain KR5 -

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Basic information

Entry
Database: PDB / ID: 8roq
TitleFAdV-C4 Aviadenovirus structure, strain KR5
Components
  • Hexon protein
  • PIIIa
  • Penton protein
  • Pre-hexon-linking protein VIII
KeywordsVIRUS / adenovirus / fowl / highly thermostable
Function / homology
Function and homology information


hexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / microtubule-dependent intracellular transport of viral material towards nucleus / viral capsid / host cell / endocytosis involved in viral entry into host cell / symbiont entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity
Similarity search - Function
Pre-hexon-linking protein IIIa / Pre-hexon-linking protein IIIa, N-terminal / Hexon-associated protein (IIIa) / Pre-hexon-linking protein VIII / Adenovirus Pll, hexon, subdomain 3 / Adenovirus hexon associated protein, protein VIII / Adenovirus Pll, hexon, N-terminal / Adenovirus Pll, hexon, C-terminal / Adenovirus Pll, hexon, subdomain 2 / Hexon, adenovirus major coat protein, N-terminal domain ...Pre-hexon-linking protein IIIa / Pre-hexon-linking protein IIIa, N-terminal / Hexon-associated protein (IIIa) / Pre-hexon-linking protein VIII / Adenovirus Pll, hexon, subdomain 3 / Adenovirus hexon associated protein, protein VIII / Adenovirus Pll, hexon, N-terminal / Adenovirus Pll, hexon, C-terminal / Adenovirus Pll, hexon, subdomain 2 / Hexon, adenovirus major coat protein, N-terminal domain / Hexon, adenovirus major coat protein, C-terminal domain / Adenovirus penton base protein / Adenovirus penton base protein / Group II dsDNA virus coat/capsid protein
Similarity search - Domain/homology
PIIIa / Penton protein / Hexon protein / Pre-hexon-linking protein VIII
Similarity search - Component
Biological speciesFowl aviadenovirus C
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsPerez-Illana, M.P. / Schachnner, A. / Condezo, G.N. / Hernando-Perez, M. / Martinez, M. / Marabini, R. / Hess, M. / San Martin, C.
Funding support2items
OrganizationGrant numberCountry
Other privateLa Caixa Foundation (ID 100010434),La Caixa Foundation (ID 100010434),LCF/BQ/SO16/52270032)
Other governmentco-funded by the Spanish State Research Agency and the European Regional Development Fund, PID2022-136456NB-I00/ AEI/10.13039/501100011033/FEDER,UE
CitationJournal: PLoS Pathog / Year: 2025
Title: Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins.
Authors: Marta Pérez-Illana / Anna Schachner / Mercedes Hernando-Pérez / Gabriela N Condezo / Alberto Paradela / Marta Martínez / Roberto Marabini / Michael Hess / Carmen San Martín /
Abstract: High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, ...High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, the poultry pathogen fowl adenovirus serotype 4 (FAdV-C4). FAdV-C4 virions are highly thermostable, despite lacking minor coat and core proteins shown to stabilize the mast- and atadenovirus particles, having no genus-specific cementing proteins, and packaging a 25% longer genome. Unique structural features of the FAdV-C4 hexon include a large insertion at the trimer equatorial region, and a long N-terminal tail. Protein IIIa conformation is closer to atadenoviruses than to mastadenoviruses, while protein VIII diverges from all previously reported structures. We interpret these differences in light of adenovirus evolution. Finally, we discuss the possible role of core composition in determining capsid stability properties. These results enlarge our view on the structural diversity of adenoviruses, and provide useful information to counteract fowl pathogens or use non-human adenoviruses as vectors.
History
DepositionJan 12, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 29, 2025Provider: repository / Type: Initial release
Revision 1.0Jan 29, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jan 29, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hexon protein
B: Hexon protein
C: Hexon protein
D: Hexon protein
E: Hexon protein
F: Hexon protein
G: Hexon protein
H: Hexon protein
I: Hexon protein
J: Hexon protein
K: Hexon protein
L: Hexon protein
M: Penton protein
N: PIIIa
O: Pre-hexon-linking protein VIII
P: Pre-hexon-linking protein VIII


Theoretical massNumber of molelcules
Total (without water)1,450,09616
Polymers1,450,09616
Non-polymers00
Water00
1
A: Hexon protein
B: Hexon protein
C: Hexon protein
D: Hexon protein
E: Hexon protein
F: Hexon protein
G: Hexon protein
H: Hexon protein
I: Hexon protein
J: Hexon protein
K: Hexon protein
L: Hexon protein
M: Penton protein
N: PIIIa
O: Pre-hexon-linking protein VIII
P: Pre-hexon-linking protein VIII
x 60


Theoretical massNumber of molelcules
Total (without water)87,005,779960
Polymers87,005,779960
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59

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Components

#1: Protein
Hexon protein / CP-H / Protein II


Mass: 106129.789 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Fowl aviadenovirus C / References: UniProt: H8WQV9
#2: Protein Penton protein / CP-P / Penton base protein / Protein III


Mass: 57448.238 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Fowl aviadenovirus C / References: UniProt: F2VJH0
#3: Protein PIIIa / PIIIa protein


Mass: 65326.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Fowl aviadenovirus C / References: UniProt: F2VJG9
#4: Protein Pre-hexon-linking protein VIII / Pre-protein VIII / pVIII


Mass: 26882.158 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Fowl aviadenovirus C / References: UniProt: H8WQW6
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Fowl aviadenovirus C / Type: VIRUS / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Fowl aviadenovirus C / Strain: KR5
Details of virusEmpty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRUS-LIKE PARTICLE
Natural hostOrganism: Gallus gallus
Buffer solutionpH: 7.8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Calibrated magnification: 95890 X / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 40.5 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING ONLY
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 9466 / Symmetry type: POINT

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