4OJE

Crystal structure of a C-terminally truncated trimeric ectodomain of the C. elegans fusion protein EFF-1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.57 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 

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This is version 2.0 of the entry. See complete history


Literature

Structural basis of eukaryotic cell-cell fusion

Perez-Vargas, J.Krey, T.Valansi, C.Avinoam, O.Haouz, A.Jamin, M.Raveh-Barak, H.Podbilewicz, B.Rey, F.A.

(2014) Cell 157: 407-419

  • DOI: https://doi.org/10.1016/j.cell.2014.02.020
  • Primary Citation of Related Structures:  
    4OJC, 4OJD, 4OJE

  • PubMed Abstract: 

    Cell-cell fusion proteins are essential in development. Here we show that the C. elegans cell-cell fusion protein EFF-1 is structurally homologous to viral class II fusion proteins. The 2.6 Å crystal structure of the EFF-1 trimer displays the same 3D fold and quaternary conformation of postfusion class II viral fusion proteins, although it lacks a nonpolar "fusion loop," indicating that it does not insert into the target membrane. EFF-1 was previously shown to be required in both cells for fusion, and we show that blocking EFF-1 trimerization blocks the fusion reaction. Together, these data suggest that whereas membrane fusion driven by viral proteins entails leveraging of a nonpolar loop, EFF-1-driven fusion of cells entails trans-trimerization such that transmembrane segments anchored in the two opposing membranes are brought into contact at the tip of the EFF-1 trimer to then, analogous to SNARE-mediated vesicle fusion, zip the two membranes into one.


  • Organizational Affiliation

    Institut Pasteur, Unité de Virologie Structurale, 25-28 Rue du Docteur Roux, 75724 Paris Cedex 15, France; CNRS UMR 3569, 25-28 Rue du Docteur Roux, 75724 Paris Cedex 15, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
EFF-1AA [auth H]526Caenorhabditis elegansMutation(s): 0 
Gene Names: C26D10.5CELE_C26D10.5eff-1
UniProt
Find proteins for G5ECA1 (Caenorhabditis elegans)
Explore G5ECA1 
Go to UniProtKB:  G5ECA1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupG5ECA1
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

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Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranoseB [auth A]2N-Glycosylation
Glycosylation Resources
GlyTouCan:  G42666HT
GlyCosmos:  G42666HT
GlyGen:  G42666HT
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.57 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 
  • Space Group: P 63
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 106.886α = 90
b = 106.886β = 90
c = 135.62γ = 120
Software Package:
Software NamePurpose
XDSdata scaling
SHARPphasing
BUSTERrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-14
    Type: Initial release
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Database references, Derived calculations, Structure summary