2WB6

Crystal structure of AFV1-102, a protein from the Acidianus Filamentous Virus 1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.216 

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This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of Afv1-102, a Protein from the Acidianus Filamentous Virus 1.

Keller, J.Leulliot, N.Collinet, B.Campanacci, V.Cambillau, C.Pranghisvilli, D.Van Tilbeurgh, H.

(2009) Protein Sci 18: 845

  • DOI: https://doi.org/10.1002/pro.79
  • Primary Citation of Related Structures:  
    2WB6

  • PubMed Abstract: 

    Viruses infecting hyperthermophilic archaea have intriguing morphologies and genomic properties. The vast majority of their genes do not have homologs other than in other hyperthermophilic viruses, and the biology of these viruses is poorly understood. As part of a structural genomics project on the proteins of these viruses, we present here the structure of a 102 amino acid protein from acidianus filamentous virus 1 (AFV1-102). The structure shows that it is made of two identical motifs that have poor sequence similarity. Although no function can be proposed from structural analysis, tight binding of the gateway tag peptide in a groove between the two motifs suggests AFV1-102 is involved in protein protein interactions.


  • Organizational Affiliation

    Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université Paris-Sud, IFR115, UMR8619-CNRS, 91405 Orsay, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
AFV1-102130Captovirus AFV1Mutation(s): 0 
UniProt
Find proteins for Q70LC3 (Acidianus filamentous virus 1 (isolate United States/Yellowstone))
Explore Q70LC3 
Go to UniProtKB:  Q70LC3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ70LC3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.216 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.89α = 90
b = 62.89β = 90
c = 110.837γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-03-03
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance