4hj1: Difference between revisions
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The entry | ==Crystal structure of glycoprotein C from Rift Valley Fever Virus (glycosylated)== | ||
<StructureSection load='4hj1' size='340' side='right'caption='[[4hj1]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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='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> | |||
</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 == | |||
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<ref>PMID:23319635</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hj1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rift Valley fever virus]] | |||
[[Category: Dessau M]] | |||
[[Category: Modis Y]] | |||
Latest revision as of 10:01, 27 November 2024
Crystal structure of glycoprotein C from Rift Valley Fever Virus (glycosylated)Crystal structure of glycoprotein C from Rift Valley Fever Virus (glycosylated)
Structural highlights
FunctionGP_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 PubMedRift 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
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