1URZ
Low pH induced, membrane fusion conformation of the envelope protein of tick-borne encephalitis virus
Summary for 1URZ
| Entry DOI | 10.2210/pdb1urz/pdb |
| Related | 1N6G 1SVB |
| Descriptor | ENVELOPE PROTEIN (2 entities in total) |
| Functional Keywords | envelope protein, membrane fusion, virus/viral protein, virus-viral protein complex |
| Biological source | TICK-BORNE ENCEPHALITIS VIRUS |
| Cellular location | Envelope protein E: Virion membrane; Multi- pass membrane protein: Q80E47 |
| Total number of polymer chains | 6 |
| Total formula weight | 262738.55 |
| Authors | Bressanelli, S.,Rey, F.A. (deposition date: 2003-11-16, release date: 2004-01-29, Last modification date: 2024-10-23) |
| Primary citation | Bressanelli, S.,Stiasny, K.,Allison, S.L.,Stura, E.A.,Duquerroy, S.,Lescar, J.,Heinz, F.X.,Rey, F.A. Structure of a Flavivirus Envelope Glycoprotein in its Low-Ph-Induced Membrane Fusion Conformation. Embo J., 23:728-, 2004 Cited by PubMed Abstract: Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick-borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low-pH-induced conformation. We show that, in the conformational transition, the three domains of the neutral-pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low-pH-induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment. PubMed: 14963486DOI: 10.1038/SJ.EMBOJ.7600064 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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