7K5D

Ebola virus VP40 octameric ring generated by a DNA oligonucleotide

7K5D の概要

• エントリーDOI: 10.2210/pdb7k5d/pdb
• 分子名称: Matrix protein VP40, HSP DNA oligonucleotide (3 entities in total)
• 機能のキーワード: ebola virus, transformer protein, dna binding protein, matrix protein, viral protein
• 由来する生物種: Zaire ebolavirus (strain Mayinga-76) (ZEBOV); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29782.64

構造登録者

Landeras-Bueno, S.,Wasserman, H.,Salie, Z.L.,Saphire, E.O. (登録日: 2020-09-16, 公開日: 2021-04-21, 最終更新日: 2023-10-18)

主引用文献

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

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: 33852858
DOI: 10.1016/j.celrep.2021.108986

実験手法

X-RAY DIFFRACTION (1.78 Å)