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5B0V

Crystal Structure of Marburg virus VP40 Dimer

Summary for 5B0V
Entry DOI10.2210/pdb5b0v/pdb
DescriptorMatrix protein VP40, ETHANOL (3 entities in total)
Functional Keywordsmarburg virus, virus assembly protein, immunosuppression, filovirus, viral protein
Biological sourceLake Victoria marburgvirus (strain Musoke-80) (MARV)
Cellular locationVirion membrane ; Peripheral membrane protein: P35260
Total number of polymer chains2
Total formula weight72080.79
Authors
Oda, S.,Bornholdt, Z.A.,Abelson, D.M.,Saphire, E.O. (deposition date: 2015-11-05, release date: 2016-01-20, Last modification date: 2024-11-13)
Primary citationOda, S.,Noda, T.,Wijesinghe, K.J.,Halfmann, P.,Bornholdt, Z.A.,Abelson, D.M.,Armbrust, T.,Stahelin, R.V.,Kawaoka, Y.,Saphire, E.O.
Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression
J.Virol., 90:1839-1848, 2015
Cited by
PubMed Abstract: Marburg virus (MARV), a member of the filovirus family, causes severe hemorrhagic fever with up to 90% lethality. MARV matrix protein VP40 is essential for assembly and release of newly copied viruses and also suppresses immune signaling in the infected cell. Here we report the crystal structure of MARV VP40. We found that MARV VP40 forms a dimer in solution, mediated by N-terminal domains, and that formation of this dimer is essential for budding of virus-like particles. We also found the N-terminal domain to be necessary and sufficient for immune antagonism. The C-terminal domains of MARV VP40 are dispensable for immunosuppression but are required for virus assembly. The C-terminal domains are only 16% identical to those of Ebola virus, differ in structure from those of Ebola virus, and form a distinct broad and flat cationic surface that likely interacts with the cell membrane during virus assembly.
PubMed: 26656687
DOI: 10.1128/JVI.01597-15
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.81 Å)
Structure validation

238895

數據於2025-07-16公開中

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