3G7T
Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation
Summary for 3G7T
| Entry DOI | 10.2210/pdb3g7t/pdb |
| Descriptor | Envelope protein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | membrane fusion protein, envelope protein, membrane anchor, fusion loop, igc domain, beta sandwich, glycoprotein, membrane, transmembrane, virion, viral protein |
| Biological source | Dengue virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 43786.34 |
| Authors | Modis, Y. (deposition date: 2009-02-10, release date: 2009-04-21, Last modification date: 2024-11-20) |
| Primary citation | Nayak, V.,Dessau, M.,Kucera, K.,Anthony, K.,Ledizet, M.,Modis, Y. Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J.Virol., 83:4338-4344, 2009 Cited by PubMed Abstract: Dengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the "pH sensor" that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer. PubMed: 19244332DOI: 10.1128/JVI.02574-08 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
Download full validation report
