2ALA

Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.319 
  • R-Value Work: 0.267 
  • R-Value Observed: 0.272 

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This is version 1.2 of the entry. See complete history


Literature

Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus.

Roussel, A.Lescar, J.Vaney, M.C.Wengler, G.Wengler, G.Rey, F.A.

(2006) Structure 14: 75-86

  • DOI: https://doi.org/10.1016/j.str.2005.09.014
  • Primary Citation of Related Structures:  
    2ALA

  • PubMed Abstract: 

    Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.


  • Organizational Affiliation

    Laboratoire de Virologie Moléculaire and Structurale, UMR 2472/1157 CNRS-INRA and IFR 115, 91198 Gif-sur-Yvette Cedex, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Structural polyprotein (P130)391Semliki Forest virusMutation(s): 0 
UniProt
Find proteins for P03315 (Semliki forest virus)
Explore P03315 
Go to UniProtKB:  P03315
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03315
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.319 
  • R-Value Work: 0.267 
  • R-Value Observed: 0.272 
  • Space Group: P 64 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.38α = 90
b = 79.38β = 90
c = 335.91γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALEPACKdata scaling
MLPHAREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-01-17
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Refinement description, Version format compliance