4LDB
Crystal Structure of Ebola Virus VP40 Dimer
Summary for 4LDB
| Entry DOI | 10.2210/pdb4ldb/pdb |
| Related | 4LD8 4LDD 4LDI 4LDM |
| Descriptor | Matrix protein VP40 (1 entity in total) |
| Functional Keywords | viral matrix protein, viral budding, assembly, viral transcription regulation, viral protein |
| Biological source | Ebola virus (ZEBOV) |
| Cellular location | Virion membrane; Peripheral membrane protein: Q05128 |
| Total number of polymer chains | 4 |
| Total formula weight | 128976.84 |
| Authors | Bornholdt, Z.A.,Ableson, D.M.,Saphire, E.O. (deposition date: 2013-06-24, release date: 2013-08-21, Last modification date: 2024-02-28) |
| Primary citation | Bornholdt, Z.A.,Noda, T.,Abelson, D.M.,Halfmann, P.,Wood, M.R.,Kawaoka, Y.,Saphire, E.O. Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle. Cell(Cambridge,Mass.), 154:763-774, 2013 Cited by PubMed Abstract: Proteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multilayered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle and demonstrate how a single wild-type, unmodified polypeptide can assemble into different structures for different functions. PubMed: 23953110DOI: 10.1016/j.cell.2013.07.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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