6egu

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'''Unreleased structure'''
 
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The entry 6egu is ON HOLD until Sep 12 2019
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==Structure of RVFV envelope protein Gc in postfusion conformation in complex with 1,2-dipropionyl-sn-glycero-3-phosphocholine==
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<StructureSection load='6egu' size='340' side='right'caption='[[6egu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6egu]] 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=6EGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EGU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=43Y:[(2R)-3-[OXIDANYL-[2-(TRIMETHYL-$L^{4}-AZANYL)ETHOXY]PHOSPHORYL]OXY-2-PROPANOYLOXY-PROPYL]+PROPANOATE'>43Y</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6egu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6egu OCA], [https://pdbe.org/6egu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6egu RCSB], [https://www.ebi.ac.uk/pdbsum/6egu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6egu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: GUARDADO-CALVO, P., REY, F.A.
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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>
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Description: Structure of RVFV envelope protein Gc in postfusion conformation in complex with 1,2-dipropionyl-sn-glycero-3-phosphocholine
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Guardado-Calvo, P]]
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<div class="pdbe-citations 6egu" style="background-color:#fffaf0;"></div>
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[[Category: Rey, F.A]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rift Valley fever virus]]
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[[Category: Guardado-Calvo P]]
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[[Category: Rey FA]]

Current revision

Structure of RVFV envelope protein Gc in postfusion conformation in complex with 1,2-dipropionyl-sn-glycero-3-phosphocholine

PDB ID 6egu

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