View source for 4cyl


==Tomographic subvolume average of EFF-1 fusogen on extracellular vesicles==
<SX load='4cyl' size='340' side='right' viewer='molstar' caption='[[4cyl]], [[Resolution|resolution]] 22.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 22.2&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/G5ECA1_CAEEL G5ECA1_CAEEL] 
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== 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<ref>PMID:24867324</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Grunewald K]]
[[Category: Siebert CA]]
[[Category: Vasishtan D]]
[[Category: Zeev-Ben-Mordehai T]]