4CYL

Tomographic subvolume average of EFF-1 fusogen on extracellular vesicles

Summary for 4CYL

• Entry DOI: 10.2210/pdb4cyl/pdb
• EMDB information: 2530
• Descriptor: EFF-1A (1 entity in total)
• Functional Keywords: cell adhesion, cell-cell fusion, extracellular fusion, membrane fusion, pre-fusion state
• Biological source: CAENORHABDITIS ELEGANS
• Total number of polymer chains: 1
• Total formula weight: 74497.14

Authors

Zeev-Ben-Mordehai, T.,Vasishtan, D.,Siebert, C.A.,Grunewald, K. (deposition date: 2014-04-13, release date: 2014-06-04, Last modification date: 2024-10-16)

Primary citation

Zeev-Ben-Mordehai, T.,Vasishtan, D.,Siebert, C.A.,Grunewald, K.
The Full-Length Cell-Cell Fusogen Eff-1 is Monomeric and Upright on the Membrane.
Nat.Commun., 5:3912-, 2014

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, 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.

PubMed: 24867324
DOI: 10.1038/NCOMMS4912

Experimental method

ELECTRON MICROSCOPY (22.2 Å)