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7JZJ

Crystal structure demonstrating CTD-CTD interactions of Zaire Ebola virus VP40 dimer

Summary for 7JZJ
Entry DOI10.2210/pdb7jzj/pdb
DescriptorMatrix protein VP40, PENTAETHYLENE GLYCOL (3 entities in total)
Functional Keywordsvp40, matrix protein, ebola virus, viral protein
Biological sourceZaire ebolavirus (strain Mayinga-76) (ZEBOV)
Total number of polymer chains4
Total formula weight129631.37
Authors
Norris, M.J.,Bornholdt, Z.A.,Saphire, E.O. (deposition date: 2020-09-02, release date: 2020-10-28, Last modification date: 2024-10-23)
Primary citationWan, W.,Clarke, M.,Norris, M.J.,Kolesnikova, L.,Koehler, A.,Bornholdt, Z.A.,Becker, S.,Ollman-Saphire, E.,Briggs, J.A.
Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers.
Elife, 9:-, 2020
Cited by
PubMed Abstract: Filoviruses such as Ebola and Marburg virus bud from the host membrane as enveloped virions. This process is achieved by the matrix protein VP40. When expressed alone, VP40 induces budding of filamentous virus-like particles, suggesting that localization to the plasma membrane, oligomerization into a matrix layer, and generation of membrane curvature are intrinsic properties of VP40. There has been no direct information on the structure of VP40 matrix layers within viruses or virus-like particles. We present structures of Ebola and Marburg VP40 matrix layers in intact virus-like particles, and within intact Marburg viruses. VP40 dimers assemble extended chains via C-terminal domain interactions. These chains stack to form 2D matrix lattices below the membrane surface. These lattices form a patchwork assembly across the membrane and suggesting that assembly may begin at multiple points. Our observations define the structure and arrangement of the matrix protein layer that mediates formation of filovirus particles.
PubMed: 33016878
DOI: 10.7554/eLife.59225
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.46 Å)
Structure validation

245663

数据于2025-12-03公开中

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