7K5D
Ebola virus VP40 octameric ring generated by a DNA oligonucleotide
Summary for 7K5D
| Entry DOI | 10.2210/pdb7k5d/pdb |
| Descriptor | Matrix protein VP40, HSP DNA oligonucleotide (3 entities in total) |
| Functional Keywords | ebola virus, transformer protein, dna binding protein, matrix protein, viral protein |
| Biological source | Zaire ebolavirus (strain Mayinga-76) (ZEBOV) More |
| Total number of polymer chains | 2 |
| Total formula weight | 29782.64 |
| Authors | Landeras-Bueno, S.,Wasserman, H.,Salie, Z.L.,Saphire, E.O. (deposition date: 2020-09-16, release date: 2021-04-21, Last modification date: 2023-10-18) |
| Primary citation | Landeras-Bueno, S.,Wasserman, H.,Oliveira, G.,VanAernum, Z.L.,Busch, F.,Salie, Z.L.,Wysocki, V.H.,Andersen, K.,Saphire, E.O. Cellular mRNA triggers structural transformation of Ebola virus matrix protein VP40 to its essential regulatory form. Cell Rep, 35:108986-108986, 2021 Cited by PubMed Abstract: The Ebola virus matrix protein VP40 forms distinct structures linked to distinct functions in the virus life cycle. Dimeric VP40 is a structural protein associated with virus assembly, while octameric, ring-shaped VP40 is associated with transcriptional control. In this study, we show that suitable nucleic acid is sufficient to trigger a dynamic transformation of VP40 dimer into the octameric ring. Deep sequencing reveals a binding preference of the VP40 ring for the 3' untranslated region of cellular mRNA and a guanine- and adenine-rich binding motif. Complementary analyses of the nucleic-acid-induced VP40 ring by native mass spectrometry, electron microscopy, and X-ray crystal structures at 1.8 and 1.4 Å resolution reveal the stoichiometry of RNA binding, as well as an interface involving a key guanine nucleotide. The host factor-induced structural transformation of protein structure in response to specific RNA triggers in the Ebola virus life cycle presents unique opportunities for therapeutic inhibition. PubMed: 33852858DOI: 10.1016/j.celrep.2021.108986 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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