3LJ5

Full Length Bacteriophage P22 Portal Protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 7.50 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.193 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Three-dimensional structure of a viral genome-delivery portal vertex.

Olia, A.S.Prevelige, P.E.Johnson, J.E.Cingolani, G.

(2011) Nat Struct Mol Biol 18: 597-603

  • DOI: https://doi.org/10.1038/nsmb.2023
  • Primary Citation of Related Structures:  
    3LJ5, 4V4K

  • PubMed Abstract: 

    DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Here, we report two snapshots of the dodecameric portal protein of bacteriophage P22. The 3.25-Å-resolution structure of the portal-protein core bound to 12 copies of gene product 4 (gp4) reveals a ~1.1-MDa assembly formed by 24 proteins. Unexpectedly, a lower-resolution structure of the full-length portal protein unveils the unique topology of the C-terminal domain, which forms a ~200-Å-long α-helical barrel. This domain inserts deeply into the virion and is highly conserved in the Podoviridae family. We propose that the barrel domain facilitates genome spooling onto the interior surface of the capsid during genome packaging and, in analogy to a rifle barrel, increases the accuracy of genome ejection into the host cell.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Portal protein
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L
725Lederbergvirus P22Mutation(s): 0 
Gene Names: 1gp1
UniProt
Find proteins for P26744 (Salmonella phage P22)
Explore P26744 
Go to UniProtKB:  P26744
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26744
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 7.50 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.193 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 408.949α = 90
b = 408.949β = 90
c = 260.009γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-20
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-03-27
    Changes: Database references
  • Version 1.3: 2024-02-21
    Changes: Data collection, Database references