5VU2
Electron cryo-microscopy of "immature" Chikungunya VLP
Summary for 5VU2
| Entry DOI | 10.2210/pdb5vu2/pdb |
| EMDB information | 8734 |
| Descriptor | E1 envelope glycoprotein, E3 envelope glycoprotein, capsid protein, ... (5 entities in total) |
| Functional Keywords | chikungunya, virus, immature, virus like particle |
| Biological source | Chikungunya virus strain Senegal 37997 (CHIKV) More |
| Total number of polymer chains | 24 |
| Total formula weight | 911444.03 |
| Authors | Rossmann, M.G.,Yap, M.L. (deposition date: 2017-05-18, release date: 2017-12-06, Last modification date: 2024-10-16) |
| Primary citation | Yap, M.L.,Klose, T.,Urakami, A.,Hasan, S.S.,Akahata, W.,Rossmann, M.G. Structural studies of Chikungunya virus maturation. Proc. Natl. Acad. Sci. U.S.A., 114:13703-13707, 2017 Cited by PubMed Abstract: Cleavage of the alphavirus precursor glycoprotein p62 into the E2 and E3 glycoproteins before assembly with the nucleocapsid is the key to producing fusion-competent mature spikes on alphaviruses. Here we present a cryo-EM, 6.8-Å resolution structure of an "immature" Chikungunya virus in which the cleavage site has been mutated to inhibit proteolysis. The spikes in the immature virus have a larger radius and are less compact than in the mature virus. Furthermore, domains B on the E2 glycoproteins have less freedom of movement in the immature virus, keeping the fusion loops protected under domain B. In addition, the nucleocapsid of the immature virus is more compact than in the mature virus, protecting a conserved ribosome-binding site in the capsid protein from exposure. These differences suggest that the posttranslational processing of the spikes and nucleocapsid is necessary to produce infectious virus. PubMed: 29203665DOI: 10.1073/pnas.1713166114 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.8 Å) |
Structure validation
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