1ES6
CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS
Summary for 1ES6
| Entry DOI | 10.2210/pdb1es6/pdb |
| Descriptor | MATRIX PROTEIN VP40 (2 entities in total) |
| Functional Keywords | beta sandwich, anti-parallel strands, beta sheet, helix, viral protein |
| Biological source | Ebola virus sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 31860.82 |
| Authors | Dessen, A.,Volchkov, V.,Dolnik, O.,Klenk, H.-D.,Weissenhorn, W. (deposition date: 2000-04-07, release date: 2000-08-30, Last modification date: 2024-02-07) |
| Primary citation | Dessen, A.,Volchkov, V.,Dolnik, O.,Klenk, H.D.,Weissenhorn, W. Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J., 19:4228-4236, 2000 Cited by PubMed Abstract: Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed. PubMed: 10944105DOI: 10.1093/emboj/19.16.4228 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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