6f9e: Difference between revisions
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<StructureSection load='6f9e' size='340' side='right' caption='[[6f9e]], [[Resolution|resolution]] 13.30Å' scene=''> | <StructureSection load='6f9e' size='340' side='right' caption='[[6f9e]], [[Resolution|resolution]] 13.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f9e]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F9E FirstGlance]. <br> | <table><tr><td colspan='2'>[[6f9e]] is a 12 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=6F9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F9E FirstGlance]. <br> | ||
</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=6f9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9e OCA], [http://pdbe.org/6f9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f9e RCSB], [http://www.ebi.ac.uk/pdbsum/6f9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9e ProSAT]</span></td></tr> | </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=6f9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9e OCA], [http://pdbe.org/6f9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f9e RCSB], [http://www.ebi.ac.uk/pdbsum/6f9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Entry of enveloped viruses relies on insertion of hydrophobic residues of the viral fusion protein into the host cell membrane. However, the intermediate conformations during fusion remain unknown. Here, we address the fusion mechanism of Rift Valley fever virus. We determine the crystal structure of the Gn glycoprotein and fit it with the Gc fusion protein into cryo-electron microscopy reconstructions of the virion. Our analysis reveals how the Gn shields the hydrophobic fusion loops of the Gc, preventing premature fusion. Electron cryotomography of virions interacting with membranes under acidic conditions reveals how the fusogenic Gc is activated upon removal of the Gn shield. Repositioning of the Gn allows extension of Gc and insertion of fusion loops in the outer leaflet of the target membrane. These data show early structural transitions that enveloped viruses undergo during host cell entry and indicate that analogous shielding mechanisms are utilized across diverse virus families. | |||
Shielding and activation of a viral membrane fusion protein.,Halldorsson S, Li S, Li M, Harlos K, Bowden TA, Huiskonen JT Nat Commun. 2018 Jan 24;9(1):349. doi: 10.1038/s41467-017-02789-2. PMID:29367607<ref>PMID:29367607</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6f9e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Rvfv]] | |||
[[Category: Bowden, T A]] | [[Category: Bowden, T A]] | ||
[[Category: Halldorsson, S]] | [[Category: Halldorsson, S]] | ||
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[[Category: Fusion protein]] | [[Category: Fusion protein]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
[[Category: Virus]] | [[Category: Virus]] | ||
Revision as of 09:49, 7 February 2018
Model of the Rift Valley fever virus glycoprotein hexamer type 3Model of the Rift Valley fever virus glycoprotein hexamer type 3
Structural highlights
Publication Abstract from PubMedEntry of enveloped viruses relies on insertion of hydrophobic residues of the viral fusion protein into the host cell membrane. However, the intermediate conformations during fusion remain unknown. Here, we address the fusion mechanism of Rift Valley fever virus. We determine the crystal structure of the Gn glycoprotein and fit it with the Gc fusion protein into cryo-electron microscopy reconstructions of the virion. Our analysis reveals how the Gn shields the hydrophobic fusion loops of the Gc, preventing premature fusion. Electron cryotomography of virions interacting with membranes under acidic conditions reveals how the fusogenic Gc is activated upon removal of the Gn shield. Repositioning of the Gn allows extension of Gc and insertion of fusion loops in the outer leaflet of the target membrane. These data show early structural transitions that enveloped viruses undergo during host cell entry and indicate that analogous shielding mechanisms are utilized across diverse virus families. Shielding and activation of a viral membrane fusion protein.,Halldorsson S, Li S, Li M, Harlos K, Bowden TA, Huiskonen JT Nat Commun. 2018 Jan 24;9(1):349. doi: 10.1038/s41467-017-02789-2. PMID:29367607[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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