5OAC

FLiP major capsid protein


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 1.2 of the entry. See complete history


Literature

Virus found in a boreal lake links ssDNA and dsDNA viruses.

Laanto, E.Mantynen, S.De Colibus, L.Marjakangas, J.Gillum, A.Stuart, D.I.Ravantti, J.J.Huiskonen, J.T.Sundberg, L.R.

(2017) Proc Natl Acad Sci U S A 114: 8378-8383

  • DOI: https://doi.org/10.1073/pnas.1703834114
  • Primary Citation of Related Structures:  
    5OAC

  • PubMed Abstract: 

    Viruses have impacted the biosphere in numerous ways since the dawn of life. However, the evolution, genetic, structural, and taxonomic diversity of viruses remain poorly understood, in part because sparse sampling of the virosphere has concentrated mostly on exploring the abundance and diversity of dsDNA viruses. Furthermore, viral genomes are highly diverse, and using only the current sequence-based methods for classifying viruses and studying their phylogeny is complicated. Here we describe a virus, FLiP ( Flavobacterium -infecting, lipid-containing phage), with a circular ssDNA genome and an internal lipid membrane enclosed in the icosahedral capsid. The 9,174-nt-long genome showed limited sequence similarity to other known viruses. The genetic data imply that this virus might use replication mechanisms similar to those found in other ssDNA replicons. However, the structure of the viral major capsid protein, elucidated at near-atomic resolution using cryo-electron microscopy, is strikingly similar to that observed in dsDNA viruses of the PRD1-adenovirus lineage, characterized by a major capsid protein bearing two β-barrels. The strong similarity between FLiP and another member of the structural lineage, bacteriophage PM2, extends to the capsid organization (pseudo T = 21 dextro ) despite the difference in the genetic material packaged and the lack of significant sequence similarity.


  • Organizational Affiliation

    Centre of Excellence in Biological Interactions, Department of Biological and Environmental Science, University of Jyväskylä, 40014 Jyväskylä, Finland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major capsid protein
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
310Bacteriophage sp.Mutation(s): 0 
UniProt
Find proteins for A0A2D0TC94 (Bacteriophage sp)
Explore A0A2D0TC94 
Go to UniProtKB:  A0A2D0TC94
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A2D0TC94
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2.0
MODEL REFINEMENTPHENIX1.11.1

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-07-26
    Type: Initial release
  • Version 1.1: 2017-08-09
    Changes: Data collection, Database references, Refinement description
  • Version 1.2: 2019-11-13
    Changes: Data collection, Other