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| | <StructureSection load='4hj1' size='340' side='right'caption='[[4hj1]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4hj1' size='340' side='right'caption='[[4hj1]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hj1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rvfv Rvfv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HJ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hj1]] is a 4 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=4HJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HJ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hjc|4hjc]]</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=4hj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hj1 OCA], [https://pdbe.org/4hj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hj1 RCSB], [https://www.ebi.ac.uk/pdbsum/4hj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hj1 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=4hj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hj1 OCA], [http://pdbe.org/4hj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hj1 RCSB], [http://www.ebi.ac.uk/pdbsum/4hj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hj1 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rvfv]] | + | [[Category: Rift Valley fever virus]] |
| - | [[Category: Dessau, M]] | + | [[Category: Dessau M]] |
| - | [[Category: Modis, Y]] | + | [[Category: Modis Y]] |
| - | [[Category: Class ii fusion protein]]
| + | |
| - | [[Category: Membrane fusion]]
| + | |
| - | [[Category: Viral envelope]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
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][1] [2] 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][3] [4] [5] Plays a role for virus dissemination in the mosquito.[UniProtKB:P21401][6] Plays a role for virus dissemination in mosquitoes.[UniProtKB:P21401]
Publication Abstract from PubMed
Rift Valley fever virus (RVFV), like many other Bunyaviridae family members, is an emerging human and animal pathogen. Bunyaviruses have an outer lipid envelope bearing two glycoproteins, G(N) and G(C), required for cell entry. Bunyaviruses deliver their genome into the host-cell cytoplasm by fusing their envelope with an endosomal membrane. The molecular mechanism of this key entry step is unknown. The crystal structure of RVFV G(C) reveals a class II fusion protein architecture found previously in flaviviruses and alphaviruses. The structure identifies G(C) as the effector of membrane fusion and provides a direct view of the membrane anchor that initiates fusion. A structure of nonglycosylated G(C) reveals an extended conformation that may represent a fusion intermediate. Unanticipated similarities between G(C) and flavivirus envelope proteins reveal an evolutionary link between the two virus families and provide insights into the organization of G(C) in the outer shell of RVFV.
Crystal structure of glycoprotein C from Rift Valley fever virus.,Dessau M, Modis Y Proc Natl Acad Sci U S A. 2013 Jan 14. PMID:23319635[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huiskonen JT, Overby AK, Weber F, Grunewald K. Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers. J Virol. 2009 Apr;83(8):3762-9. doi: 10.1128/JVI.02483-08. Epub 2009 Feb 4. PMID:19193794 doi:http://dx.doi.org/10.1128/JVI.02483-08
- ↑ Dessau M, Modis Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci U S A. 2013 Jan 14. PMID:23319635 doi:http://dx.doi.org/10.1073/pnas.1217780110
- ↑ Huiskonen JT, Overby AK, Weber F, Grunewald K. Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers. J Virol. 2009 Apr;83(8):3762-9. doi: 10.1128/JVI.02483-08. Epub 2009 Feb 4. PMID:19193794 doi:http://dx.doi.org/10.1128/JVI.02483-08
- ↑ Dessau M, Modis Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci U S A. 2013 Jan 14. PMID:23319635 doi:http://dx.doi.org/10.1073/pnas.1217780110
- ↑ 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. A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion. Science. 2017 Nov 3;358(6363):663-667. doi: 10.1126/science.aal2712. PMID:29097548 doi:http://dx.doi.org/10.1126/science.aal2712
- ↑ Kading RC, Crabtree MB, Bird BH, Nichol ST, Erickson BR, Horiuchi K, Biggerstaff BJ, Miller BR. Deletion of the NSm virulence gene of Rift Valley fever virus inhibits virus replication in and dissemination from the midgut of Aedes aegypti mosquitoes. PLoS Negl Trop Dis. 2014 Feb 13;8(2):e2670. doi: 10.1371/journal.pntd.0002670., eCollection 2014 Feb. PMID:24551252 doi:http://dx.doi.org/10.1371/journal.pntd.0002670
- ↑ Dessau M, Modis Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci U S A. 2013 Jan 14. PMID:23319635 doi:http://dx.doi.org/10.1073/pnas.1217780110
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