4OJE

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

Summary for 4OJE

• Entry DOI: 10.2210/pdb4oje/pdb
• Related: 4OJC 4OJD
• Descriptor: EFF-1A, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: class ii fusion protein, membrane fusion protein, cell surface, membrane protein
• Biological source: Caenorhabditis elegans (nematode)
• Total number of polymer chains: 1
• Total formula weight: 60067.29

Authors

Krey, T.,Rey, F.A. (deposition date: 2014-01-21, release date: 2014-05-14, Last modification date: 2024-10-30)

Primary citation

Perez-Vargas, J.,Krey, T.,Valansi, C.,Avinoam, O.,Haouz, A.,Jamin, M.,Raveh-Barak, H.,Podbilewicz, B.,Rey, F.A.
Structural basis of eukaryotic cell-cell fusion
Cell(Cambridge,Mass.), 157:407-419, 2014

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.

PubMed: 24725407
DOI: 10.1016/j.cell.2014.02.020

Experimental method

X-RAY DIFFRACTION (2.57 Å)