Summary for 5I2S
| Entry DOI | 10.2210/pdb5i2s/pdb |
| Descriptor | Glycoprotein G, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | virion protein, membrane protein, envelope protein, membrane fusion, viral protein |
| Biological source | Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV) |
| Cellular location | Virion membrane ; Single-pass type I membrane protein : P0C2X0 |
| Total number of polymer chains | 1 |
| Total formula weight | 48333.73 |
| Authors | Roche, S.,Bressanelli, S. (deposition date: 2016-02-09, release date: 2016-03-02, Last modification date: 2024-10-16) |
| Primary citation | Roche, S.,Rey, F.A.,Gaudin, Y.,Bressanelli, S. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science, 315:843-848, 2007 Cited by PubMed Abstract: Glycoprotein G of the vesicular stomatitis virus triggers membrane fusion via a low pH-induced structural rearrangement. Despite the equilibrium between the pre- and postfusion states, the structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G. Comparison with the structure of the postfusion form suggests a pathway for the conformational change. In the prefusion form, G has the shape of a tripod with the fusion loops exposed, which point toward the viral membrane, and with the antigenic sites located at the distal end of the molecule. A large number of G glycoproteins, perhaps organized as in the crystals, act cooperatively to induce membrane merging. PubMed: 17289996DOI: 10.1126/SCIENCE.1135710 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
