6C54
Ebola nucleoprotein nucleocapsid-like assembly and the asymmetric unit
Summary for 6C54
Entry DOI | 10.2210/pdb6c54/pdb |
EMDB information | 7343 |
Descriptor | Nucleoprotein (1 entity in total) |
Functional Keywords | ebola, nucleoprotein, nucleocapsid, helical reconstruction, rna binding protein |
Biological source | Zaire ebolavirus |
Total number of polymer chains | 2 |
Total formula weight | 96285.18 |
Authors | Su, Z.,Wu, C.,Pintilie, G.D.,Chiu, W.,Amarasinghe, G.K.,Leung, D.W. (deposition date: 2018-01-13, release date: 2018-03-07, Last modification date: 2024-03-13) |
Primary citation | 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 Cited by 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: 29474922DOI: 10.1016/j.cell.2018.02.009 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (5.8 Å) |
Structure validation
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