3ZN6

VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.53 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Bacteriophage P23-77 Capsid Protein Structures Reveal the Archetype of an Ancient Branch from a Major Virus Lineage.

Rissanen, I.Grimes, J.M.Pawlowski, A.Mantynen, S.Harlos, K.Bamford, J.K.H.Stuart, D.I.

(2013) Structure 21: 718

  • DOI: https://doi.org/10.1016/j.str.2013.02.026
  • Primary Citation of Related Structures:  
    3ZMN, 3ZMO, 3ZN4, 3ZN5, 3ZN6

  • PubMed Abstract: 

    It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 Å resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid architecture and viral assembly, quite different from previously published models. The structures of the capsid proteins and their mode of association to form the viral capsid suggest that the P23-77-like and adeno-PRD1 lineages of viruses share an extremely ancient common ancestor.


  • Organizational Affiliation

    Department of Biological and Environmental Science and Nanoscience Center, University of Jyväskylä, Jyväskylä 40014, Finland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
VP17291Thermus virus P23-77Mutation(s): 0 
UniProt
Find proteins for C8CHL5 (Thermus virus P23-77)
Explore C8CHL5 
Go to UniProtKB:  C8CHL5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC8CHL5
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
VP16173Thermus virus P23-77Mutation(s): 0 
UniProt
Find proteins for C8CHL4 (Thermus virus P23-77)
Explore C8CHL4 
Go to UniProtKB:  C8CHL4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC8CHL4
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.53 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.78α = 90
b = 69.61β = 104.99
c = 81.62γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
xia2data reduction
XDSdata reduction
xia2data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-05-15
    Type: Initial release
  • Version 1.1: 2013-05-22
    Changes: Database references
  • Version 1.2: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description