6C54

Ebola nucleoprotein nucleocapsid-like assembly and the asymmetric unit

6C54 の概要

• エントリーDOI: 10.2210/pdb6c54/pdb
• EMDBエントリー: 7343
• 分子名称: Nucleoprotein (1 entity in total)
• 機能のキーワード: ebola, nucleoprotein, nucleocapsid, helical reconstruction, rna binding protein
• 由来する生物種: Zaire ebolavirus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96285.18

構造登録者

Su, Z.,Wu, C.,Pintilie, G.D.,Chiu, W.,Amarasinghe, G.K.,Leung, D.W. (登録日: 2018-01-13, 公開日: 2018-03-07, 最終更新日: 2024-03-13)

主引用文献

Su, Z.,Wu, C.,Shi, L.,Luthra, P.,Pintilie, G.D.,Johnson, B.,Porter, J.R.,Ge, P.,Chen, M.,Liu, G.,Frederick, T.E.,Binning, J.M.,Bowman, G.R.,Zhou, Z.H.,Basler, C.F.,Gross, M.L.,Leung, D.W.,Chiu, W.,Amarasinghe, G.K.
Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.
Cell, 172:966-978.e12, 2018

PubMed Abstract: Ebola virus nucleoprotein (eNP) assembles into higher-ordered structures that form the viral nucleocapsid (NC) and serve as the scaffold for viral RNA synthesis. However, molecular insights into the NC assembly process are lacking. Using a hybrid approach, we characterized the NC-like assembly of eNP, identified novel regulatory elements, and described how these elements impact function. We generated a three-dimensional structure of the eNP NC-like assembly at 5.8 Å using electron cryo-microscopy and identified a new regulatory role for eNP helices α22-α23. Biochemical, biophysical, and mutational analyses revealed that inter-eNP contacts within α22-α23 are critical for viral NC assembly and regulate viral RNA synthesis. These observations suggest that the N terminus and α22-α23 of eNP function as context-dependent regulatory modules (CDRMs). Our current study provides a framework for a structural mechanism for NC-like assembly and a new therapeutic target.

PubMed: 29474922
DOI: 10.1016/j.cell.2018.02.009

実験手法

ELECTRON MICROSCOPY (5.8 Å)