4UFT

Structure of the helical Measles virus nucleocapsid

Summary for 4UFT

• Entry DOI: 10.2210/pdb4uft/pdb
• EMDB information: 2867
• Descriptor: NUCLEOPROTEIN, 5'-R(*CP*CP*CP*CP*CP*CP)-3' (2 entities in total)
• Functional Keywords: rna binding protein, measles virus nucleocapsid, transcription and replication template
• Biological source: MEASLES VIRUS STRAIN HALLE; More
• Total number of polymer chains: 2
• Total formula weight: 45292.75

Authors

Gutsche, I.,Desfosses, A.,Effantin, G.,Ling, W.L.,Haupt, M.,Ruigrok, R.W.H.,Sachse, C.,Schoehn, G. (deposition date: 2015-03-19, release date: 2015-04-29, Last modification date: 2024-05-08)

Primary citation

Gutsche, I.,Desfosses, A.,Effantin, G.,Ling, W.L.,Haupt, M.,Ruigrok, R.W.H.,Sachse, C.,Schoehn, G.
Near-Atomic Cryo-Em Structure of the Helical Measles Virus Nucleocapsid.
Science, 348:704-, 2015

PubMed Abstract: 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.

PubMed: 25883315
DOI: 10.1126/SCIENCE.AAA5137

Experimental method

ELECTRON MICROSCOPY (4.3 Å)