Papageorgiou N., Coutard B., Lantez V., Gautron E., Chauvet O., Baronti Cécile, Norder H., de Lamballerie Xavier, Heresanu V., Ferte N., Veesler S., Gorbalenya A. E., Canard B. (2010). The 2C putative helicase of echovirus 30 adopts a hexameric ring-shaped structure. Acta Crystallographica Section D. Biological Crystallography, 66 (Part 10), p. 1116-1120. ISSN 0907-4449.
Titre du document
The 2C putative helicase of echovirus 30 adopts a hexameric ring-shaped structure
Année de publication
2010
Auteurs
Papageorgiou N., Coutard B., Lantez V., Gautron E., Chauvet O., Baronti Cécile, Norder H., de Lamballerie Xavier, Heresanu V., Ferte N., Veesler S., Gorbalenya A. E., Canard B.
Source
Acta Crystallographica Section D. Biological Crystallography, 2010,
66 (Part 10), p. 1116-1120 ISSN 0907-4449
The 2C protein, which is an essential ATPase and one of the most conserved proteins across the Picornaviridae family, is an emerging antiviral target for which structural and functional characterization remain elusive. Based on a distant relationship to helicases of small DNA viruses, piconavirus 2C proteins have been predicted to unwind double-stranded RNAs. Here, a terminally extended variant of the 2C protein from echovirus 30 has been studied by means of enzymatic activity assays, transmission electron microscopy, atomic force microscopy and dynamic light scattering. The transmission electron-microscopy technique showed the existence of ring-shaped particles with similar to 12 nm external diameter. Image analysis revealed that these particles were hexameric and resembled those formed by superfamily 3 DNA virus helicases.
Plan de classement
Sciences fondamentales / Techniques d'analyse et de recherche [020]
Localisation
Fonds IRD [F B010052867]
Identifiant IRD
fdi:010052867
