4HJC

Crystal structure of glycoprotein C from Rift Valley Fever Virus (non-glycosylated)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.15 Å
  • R-Value Free: 0.311 
  • R-Value Work: 0.259 
  • R-Value Observed: 0.262 

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This is version 1.3 of the entry. See complete history


Literature

Crystal structure of glycoprotein C from Rift Valley fever virus.

Dessau, M.Modis, Y.

(2013) Proc Natl Acad Sci U S A 110: 1696-1701

  • DOI: https://doi.org/10.1073/pnas.1217780110
  • Primary Citation of Related Structures:  
    4HJ1, 4HJC

  • PubMed Abstract: 

    Rift Valley fever virus (RVFV), like many other Bunyaviridae family members, is an emerging human and animal pathogen. Bunyaviruses have an outer lipid envelope bearing two glycoproteins, G(N) and G(C), required for cell entry. Bunyaviruses deliver their genome into the host-cell cytoplasm by fusing their envelope with an endosomal membrane. The molecular mechanism of this key entry step is unknown. The crystal structure of RVFV G(C) reveals a class II fusion protein architecture found previously in flaviviruses and alphaviruses. The structure identifies G(C) as the effector of membrane fusion and provides a direct view of the membrane anchor that initiates fusion. A structure of nonglycosylated G(C) reveals an extended conformation that may represent a fusion intermediate. Unanticipated similarities between G(C) and flavivirus envelope proteins reveal an evolutionary link between the two virus families and provide insights into the organization of G(C) in the outer shell of RVFV.


  • Organizational Affiliation

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ENVELOPE GLYCOPROTEIN428Rift Valley fever virusMutation(s): 0 
UniProt
Find proteins for P03518 (Rift valley fever virus)
Explore P03518 
Go to UniProtKB:  P03518
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03518
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.15 Å
  • R-Value Free: 0.311 
  • R-Value Work: 0.259 
  • R-Value Observed: 0.262 
  • Space Group: P 64 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 114.347α = 90
b = 114.347β = 90
c = 170.675γ = 120
Software Package:
Software NamePurpose
SCALEPACKdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection
DENZOdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-01-16
    Type: Initial release
  • Version 1.1: 2013-01-30
    Changes: Database references
  • Version 1.2: 2013-02-13
    Changes: Database references
  • Version 1.3: 2017-11-15
    Changes: Refinement description