7ETM

C6 portal vertex in the enveloped virion capsid

  • Classification: VIRAL PROTEIN
  • Organism(s): Human betaherpesvirus 5
  • Mutation(s): No 

  • Deposited: 2021-05-13 Released: 2021-07-14 
  • Deposition Author(s): Li, Z., Yu, X.
  • Funding Organization(s): National Natural Science Foundation of China (NSFC)

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis for genome packaging, retention, and ejection in human cytomegalovirus.

Li, Z.Pang, J.Dong, L.Yu, X.

(2021) Nat Commun 12: 4538-4538

  • DOI: https://doi.org/10.1038/s41467-021-24820-3
  • Primary Citation of Related Structures:  
    7ET2, 7ET3, 7ETJ, 7ETM, 7ETO

  • PubMed Abstract: 

    How the human cytomegalovirus (HCMV) genome-the largest among human herpesviruses-is packaged, retained, and ejected remains unclear. We present the in situ structures of the symmetry-mismatched portal and the capsid vertex-specific components (CVSCs) of HCMV. The 5-fold symmetric 10-helix anchor-uncommon among known portals-contacts the portal-encircling DNA, which is presumed to squeeze the portal as the genome packaging proceeds. We surmise that the 10-helix anchor dampens this action to delay the portal reaching a "head-full" packaging state, thus facilitating the large genome to be packaged. The 6-fold symmetric turret, latched via a coiled coil to a helix from a major capsid protein, supports the portal to retain the packaged genome. CVSCs at the penton vertices-presumed to increase inner capsid pressure-display a low stoichiometry, which would aid genome retention. We also demonstrate that the portal and capsid undergo conformational changes to facilitate genome ejection after viral cell entry.


  • Organizational Affiliation

    Cryo-Electron Microscopy Research Center, the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Portal protein697Human betaherpesvirus 5Mutation(s): 0 
UniProt
Find proteins for P16735 (Human cytomegalovirus (strain AD169))
Explore P16735 
Go to UniProtKB:  P16735
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP16735
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data

  • Released Date: 2021-07-14 
  • Deposition Author(s): Li, Z., Yu, X.

Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China31900869

Revision History  (Full details and data files)

  • Version 1.0: 2021-07-14
    Type: Initial release
  • Version 1.1: 2021-08-18
    Changes: Database references
  • Version 1.2: 2024-06-05
    Changes: Data collection