6YBA

HAdV-F41 Capsid


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses.

Perez-Illana, M.Martinez, M.Condezo, G.N.Hernando-Perez, M.Mangroo, C.Brown, M.Marabini, R.San Martin, C.

(2021) Sci Adv 7

  • DOI: 10.1126/sciadv.abd9421
  • Primary Citation of Related Structures:  
    6YBA

  • PubMed Abstract: 
  • Enteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-Å-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms ...

    Enteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-Å-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms. While the overall structures of hexon, penton base, and internal minor coat proteins IIIa and VIII are conserved, we observe partially ordered elements reinforcing the vertex region, which suggests their role in enhancing the physicochemical capsid stability of HAdV-F41. Unexpectedly, we find an organization of the external minor coat protein IX different from all previously characterized human and nonhuman mastadenoviruses. Knowledge of the structure of enteric adenoviruses provides a starting point for the design of vectors suitable for oral delivery or intestinal targeting.


    Organizational Affiliation

    Department of Macromolecular Structures, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain. carmen@cnb.csic.es.



Macromolecules
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Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Hexon protein
A, B, C, D, E, F, G, H, I, J, K, L
A, B, C, D, E, F, G, H, I, J, K, L
925Human adenovirus 41Mutation(s): 0 
Gene Names: L3
UniProt
Find proteins for P11820 (Human adenovirus F serotype 41)
Explore P11820 
Go to UniProtKB:  P11820
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UniProt GroupP11820
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Entity ID: 2
MoleculeChainsSequence LengthOrganismDetailsImage
Penton proteinM508Human adenovirus 41Mutation(s): 0 
Gene Names: L2
UniProt
Find proteins for Q9QAH8 (Human adenovirus F serotype 41)
Explore Q9QAH8 
Go to UniProtKB:  Q9QAH8
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UniProt GroupQ9QAH8
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Entity ID: 3
MoleculeChainsSequence LengthOrganismDetailsImage
Pre-hexon-linking protein IIIaN579Human adenovirus 41Mutation(s): 0 
Gene Names: L1 IIIa
UniProt
Find proteins for Q67716 (Human adenovirus F serotype 41)
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UniProt GroupQ67716
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Entity ID: 4
MoleculeChainsSequence LengthOrganismDetailsImage
Pre-hexon-linking protein VIIIO, P233Human adenovirus 41Mutation(s): 0 
Gene Names: L4
UniProt
Find proteins for P11822 (Human adenovirus F serotype 41)
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UniProt GroupP11822
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Entity ID: 5
MoleculeChainsSequence LengthOrganismDetailsImage
Hexon-interlacing proteinQ, R, S, T133Human adenovirus 41Mutation(s): 0 
Gene Names: IX
UniProt
Find proteins for P32539 (Human adenovirus F serotype 41)
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Entity ID: 6
MoleculeChainsSequence LengthOrganismDetailsImage
Pre-protein VIU,
V,
X [auth Y],
Y [auth u]
266Human adenovirus 41Mutation(s): 0 
Gene Names: L3
UniProt
Find proteins for P16139 (Human adenovirus F serotype 41)
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UniProt GroupP16139
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Entity ID: 7
MoleculeChainsSequence LengthOrganismDetailsImage
Pre-histone-like nucleoproteinW,
Z [auth w]
183Human adenovirus 41Mutation(s): 0 
Gene Names: L2
UniProt
Find proteins for B5SNS1 (Human adenovirus F serotype 41)
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UniProt GroupB5SNS1
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report




Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Spanish Ministry of Science, Innovation, and UniversitiesSpainBFU-2016-74868P
Spanish Ministry of Science, Innovation, and UniversitiesSpainBIO2016-76400-R
European CommissionEuropean Unioninext-1750

Revision History  (Full details and data files)

  • Version 1.0: 2021-03-10
    Type: Initial release
  • Version 1.1: 2021-03-17
    Changes: Database references