5FJL

Crystal structure of raptor adenovirus 1 fibre head, wild-type form


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.47 Å
  • R-Value Free: 0.179 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.158 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal Structure of Raptor Adenovirus 1 Fibre Head and Role of the Beta-Hairpin in Siadenovirus Fibre Head Domains

Nguyen, T.H.Ballmann, M.Z.Do, H.T.Truong, H.N.Benko, M.Harrach, B.van Raaij, M.J.

(2016) Virol J 13: 106

  • DOI: https://doi.org/10.1186/s12985-016-0558-7
  • Primary Citation of Related Structures:  
    5FJL, 5FLD

  • PubMed Abstract: 

    Most adenoviruses recognize their host cells via an interaction of their fibre head domains with a primary receptor. The structural framework of adenovirus fibre heads is conserved between the different adenovirus genera for which crystal structures have been determined (Mastadenovirus, Aviadenovirus, Atadenovirus and Siadenovirus), but genus-specific differences have also been observed. The only known siadenovirus fibre head structure, that of turkey adenovirus 3 (TAdV-3), revealed a twisted beta-sandwich resembling the reovirus fibre head architecture more than that of other adenovirus fibre heads, plus a unique beta-hairpin embracing a neighbouring monomer. The TAdV-3 fibre head was shown to bind sialyllactose.


  • Organizational Affiliation

    Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Calle Darwin 3, E-28049, Madrid, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FIBER PROTEIN174Raptor siadenovirus AMutation(s): 0 
UniProt
Find proteins for F4MI11 (Raptor adenovirus 1)
Explore F4MI11 
Go to UniProtKB:  F4MI11
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF4MI11
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.47 Å
  • R-Value Free: 0.179 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.158 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.72α = 90
b = 81.72β = 90
c = 81.72γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-06-29
    Type: Initial release
  • Version 1.1: 2016-07-06
    Changes: Database references
  • Version 1.2: 2017-12-13
    Changes: Database references
  • Version 1.3: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description