6F8P
Crystal structure of Gn from Rift Valley fever virus
Summary for 6F8P
| Entry DOI | 10.2210/pdb6f8p/pdb |
| Descriptor | Glycoprotein (2 entities in total) |
| Functional Keywords | phlebovirus, glycoprotein, bunyavirus, host cell entry, viral protein |
| Biological source | Rift valley fever virus (RVFV) |
| Total number of polymer chains | 1 |
| Total formula weight | 34958.86 |
| Authors | Halldorsson, S.,Bowden, T.A.,Harlos, K. (deposition date: 2017-12-13, release date: 2018-01-31, Last modification date: 2024-10-09) |
| Primary citation | Halldorsson, S.,Li, S.,Li, M.,Harlos, K.,Bowden, T.A.,Huiskonen, J.T. Shielding and activation of a viral membrane fusion protein. Nat Commun, 9:349-349, 2018 Cited by PubMed Abstract: 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. PubMed: 29367607DOI: 10.1038/s41467-017-02789-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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