+Search query
-Structure paper
Title | The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 5, Page 3912, Year 2014 |
Publish date | May 28, 2014 |
Authors | Tzviya Zeev-Ben-Mordehai / Daven Vasishtan / C Alistair Siebert / Kay Grünewald / |
PubMed Abstract | Fusogens are membrane proteins that remodel lipid bilayers to facilitate membrane merging. Although several fusogen ectodomain structures have been solved, structural information on full-length, ...Fusogens are membrane proteins that remodel lipid bilayers to facilitate membrane merging. Although several fusogen ectodomain structures have been solved, structural information on full-length, natively membrane-anchored fusogens is scarce. Here we present the electron cryo microscopy three-dimensional reconstruction of the Caenorhabditis elegans epithelial fusion failure 1 (EFF-1) protein natively anchored in cell-derived membrane vesicles. This reveals a membrane protruding, asymmetric, elongated monomer. Flexible fitting of a protomer of the EFF-1 crystal structure, which is homologous to viral class-II fusion proteins, shows that EFF-1 has a hairpin monomeric conformation before fusion. These structural insights, when combined with our observations of membrane-merging intermediates between vesicles, enable us to propose a model for EFF-1 mediated fusion. This process, involving identical proteins on both membranes to be fused, follows a mechanism that shares features of SNARE-mediated fusion while using the structural building blocks of the unilaterally acting class-II viral fusion proteins. |
External links | Nat Commun / PubMed:24867324 / PubMed Central |
Methods | EM (subtomogram averaging) / EM (tomography) |
Resolution | 22.2 - 45.0 Å |
Structure data | EMDB-2530, PDB-4cyl: EMDB-2531: EMDB-2532: |
Source |
|
Keywords | CELL ADHESION / CELL-CELL FUSION / EXTRACELLULAR FUSION / MEMBRANE FUSION / PRE-FUSION STATE |