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| | <StructureSection load='4ojc' size='340' side='right'caption='[[4ojc]], [[Resolution|resolution]] 2.93Å' scene=''> | | <StructureSection load='4ojc' size='340' side='right'caption='[[4ojc]], [[Resolution|resolution]] 2.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ojc]] 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=4OJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OJC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ojc]] 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=4OJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OJC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.93Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ojd|4ojd]], [[4oje|4oje]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C26D10.5, CELE_C26D10.5, eff-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4ojc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojc OCA], [https://pdbe.org/4ojc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ojc RCSB], [https://www.ebi.ac.uk/pdbsum/4ojc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ojc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojc OCA], [http://pdbe.org/4ojc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ojc RCSB], [http://www.ebi.ac.uk/pdbsum/4ojc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojc 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__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Krey, T]] | + | [[Category: Krey T]] |
| - | [[Category: Rey, F A]] | + | [[Category: Rey FA]] |
| - | [[Category: Cell surface]]
| + | |
| - | [[Category: Class ii fusion protein]]
| + | |
| - | [[Category: Membrane fusion protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
G5ECA1_CAEEL
Publication Abstract from PubMed
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 A 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.
Structural basis of eukaryotic cell-cell fusion.,Perez-Vargas J, Krey T, Valansi C, Avinoam O, Haouz A, Jamin M, Raveh-Barak H, Podbilewicz B, Rey FA Cell. 2014 Apr 10;157(2):407-19. doi: 10.1016/j.cell.2014.02.020. PMID:24725407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Perez-Vargas J, Krey T, Valansi C, Avinoam O, Haouz A, Jamin M, Raveh-Barak H, Podbilewicz B, Rey FA. Structural basis of eukaryotic cell-cell fusion. Cell. 2014 Apr 10;157(2):407-19. doi: 10.1016/j.cell.2014.02.020. PMID:24725407 doi:http://dx.doi.org/10.1016/j.cell.2014.02.020
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