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| | <SX load='4cyl' size='340' side='right' viewer='molstar' caption='[[4cyl]], [[Resolution|resolution]] 22.20Å' scene=''> | | <SX load='4cyl' size='340' side='right' viewer='molstar' caption='[[4cyl]], [[Resolution|resolution]] 22.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cyl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4CYL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cyl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CYL FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4cyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyl OCA], [http://pdbe.org/4cyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cyl RCSB], [http://www.ebi.ac.uk/pdbsum/4cyl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyl ProSAT]</span></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyl OCA], [https://pdbe.org/4cyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cyl RCSB], [https://www.ebi.ac.uk/pdbsum/4cyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/G5ECA1_CAEEL G5ECA1_CAEEL]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grunewald, K]] | + | [[Category: Grunewald K]] |
| - | [[Category: Siebert, C A]] | + | [[Category: Siebert CA]] |
| - | [[Category: Vasishtan, D]] | + | [[Category: Vasishtan D]] |
| - | [[Category: Zeev-Ben-Mordehai, T]] | + | [[Category: Zeev-Ben-Mordehai T]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell-cell fusion]]
| + | |
| - | [[Category: Extracellular fusion]]
| + | |
| - | [[Category: Membrane fusion]]
| + | |
| - | [[Category: Pre-fusion state]]
| + | |
| Structural highlights
Function
[G5ECA1_CAEEL]
Publication Abstract from PubMed
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.
The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane.,Zeev-Ben-Mordehai T, Vasishtan D, Siebert CA, Grunewald K Nat Commun. 2014 May 28;5:3912. doi: 10.1038/ncomms4912. PMID:24867324[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zeev-Ben-Mordehai T, Vasishtan D, Siebert CA, Grunewald K. The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane. Nat Commun. 2014 May 28;5:3912. doi: 10.1038/ncomms4912. PMID:24867324 doi:http://dx.doi.org/10.1038/ncomms4912
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