6egt
From Proteopedia
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==Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES== | ==Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES== | ||
| - | <StructureSection load='6egt' size='340' side='right' caption='[[6egt]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='6egt' size='340' side='right'caption='[[6egt]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6egt]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EGT OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6egt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rift_Valley_fever_virus Rift Valley fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EGT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6egt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6egt OCA], [https://pdbe.org/6egt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6egt RCSB], [https://www.ebi.ac.uk/pdbsum/6egt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6egt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GP_RVFV GP_RVFV] Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (PubMed:19193794, PubMed:23319635). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (By similarity). Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (By similarity).[UniProtKB:P09613][UniProtKB:P21401]<ref>PMID:19193794</ref> <ref>PMID:23319635</ref> Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (PubMed:23319635, PubMed:29097548). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (PubMed:19193794, PubMed:23319635). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (By similarity).[UniProtKB:P09613]<ref>PMID:19193794</ref> <ref>PMID:23319635</ref> <ref>PMID:29097548</ref> Plays a role for virus dissemination in the mosquito.[UniProtKB:P21401]<ref>PMID:24551252</ref> Plays a role for virus dissemination in mosquitoes.[UniProtKB:P21401] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Rift Valley fever virus (RVFV) is transmitted by infected mosquitoes, causing severe disease in humans and livestock across Africa. We determined the x-ray structure of the RVFV class II fusion protein Gc in its postfusion form and in complex with a glycerophospholipid (GPL) bound in a conserved cavity next to the fusion loop. Site-directed mutagenesis and molecular dynamics simulations further revealed a built-in motif allowing en bloc insertion of the fusion loop into membranes, making few nonpolar side-chain interactions with the aliphatic moiety and multiple polar interactions with lipid head groups upon membrane restructuring. The GPL head-group recognition pocket is conserved in the fusion proteins of other arthropod-borne viruses, such as Zika and chikungunya viruses, which have recently caused major epidemics worldwide. | ||
| + | |||
| + | A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion.,Guardado-Calvo P, Atkovska K, Jeffers SA, Grau N, Backovic M, Perez-Vargas J, de Boer SM, Tortorici MA, Pehau-Arnaudet G, Lepault J, England P, Rottier PJ, Bosch BJ, Hub JS, Rey FA Science. 2017 Nov 3;358(6363):663-667. doi: 10.1126/science.aal2712. PMID:29097548<ref>PMID:29097548</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6egt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rift Valley fever virus]] |
| - | [[Category: | + | [[Category: Guardado-Calvo P]] |
| - | [[Category: | + | [[Category: Rey FA]] |
Current revision
Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES
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