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TitleStructural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid.
Journal, issue, pagesScience, Vol. 348, Issue 6235, Page 704-707, Year 2015
Publish dateMay 8, 2015
AuthorsIrina Gutsche / Ambroise Desfosses / Grégory Effantin / Wai Li Ling / Melina Haupt / Rob W H Ruigrok / Carsten Sachse / Guy Schoehn /
PubMed AbstractMeasles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the structure of the helical nucleocapsid formed by the ...Measles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the structure of the helical nucleocapsid formed by the folded domain of the measles virus nucleoprotein encapsidating an RNA at a resolution of 4.3 angstroms. The resulting pseudoatomic model of the measles virus nucleocapsid offers important insights into the mechanism of the helical polymerization of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein. The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of measles virus binds six nucleotides, whereas the respiratory syncytial virus nucleoprotein binds seven. It provides a rational basis for further analysis of measles virus replication and transcription, and reveals potential targets for drug design.
External linksScience / PubMed:25883315
MethodsEM (single particle)
Resolution4.3 Å
Structure data

2867

4uft

EMDB-2867, PDB-4uft:
Structure of the helical Measles virus nucleocapsid
Method: EM (single particle) / Resolution: 4.3 Å

Source
  • Measles virus
  • measles virus strain halle
  • spodoptera frugiperda (fall armyworm)
KeywordsRNA BINDING PROTEIN / MEASLES VIRUS NUCLEOCAPSID / TRANSCRIPTION AND REPLICATION TEMPLATE

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