7C4W

Cryo-EM structure of A particle Coxsackievirus A10 at pH 5.5


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.

Cui, Y.Peng, R.Song, H.Tong, Z.Qu, X.Liu, S.Zhao, X.Chai, Y.Wang, P.Gao, G.F.Qi, J.

(2020) Proc Natl Acad Sci U S A 117: 18711-18718

  • DOI: https://doi.org/10.1073/pnas.2005341117
  • Primary Citation of Related Structures:  
    7BZN, 7BZO, 7BZT, 7BZU, 7C4T, 7C4W, 7C4Y, 7C4Z

  • PubMed Abstract: 

    KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection.


  • Organizational Affiliation

    Chinese Academy of Sciences (CAS) Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, 100101 Beijing, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP1298Coxsackievirus A10Mutation(s): 0 
UniProt
Find proteins for A0A0C5AWF6 (Coxsackievirus A10)
Explore A0A0C5AWF6 
Go to UniProtKB:  A0A0C5AWF6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0C5AWF6
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP2255Coxsackievirus A10Mutation(s): 0 
UniProt
Find proteins for G0YPI2 (Coxsackievirus A10)
Explore G0YPI2 
Go to UniProtKB:  G0YPI2
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UniProt GroupG0YPI2
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP3240Coxsackievirus A10Mutation(s): 0 
UniProt
Find proteins for G0YPI2 (Coxsackievirus A10)
Explore G0YPI2 
Go to UniProtKB:  G0YPI2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupG0YPI2
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Chinese Academy of SciencesChinaXDB29010202

Revision History  (Full details and data files)

  • Version 1.0: 2020-07-22
    Type: Initial release
  • Version 1.1: 2020-08-05
    Changes: Database references
  • Version 1.2: 2020-08-19
    Changes: Database references
  • Version 1.3: 2024-03-27
    Changes: Data collection, Database references, Derived calculations