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Papageorgiou, N., Coutard, B., Lantez, V., Gautron, E., Chauvet, O., Baronti, C., Norder, H., de Lamballerie, X., 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 Crystallogr. Sect. D-Biol. Crystallogr. 66 1116–1120. 
Added by: Laurent Cournède (2016-03-10 21:37:31)
Type de référence: Article
DOI: 10.1107/S090744491002809X
Numéro d'identification (ISBN etc.): 0907-4449
Clé BibTeX: Papageorgiou2010
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Catégories: PMN
Mots-clés: 2C protein, adenoassociated virus type-2, atpase activity, complex, crystal-structure, dna helicases, echovirus 30, hydrolysis, mechanism, poliovirus, protein 2c, replication, transmission electron microscopy
Créateurs: Baronti, Canard, Chauvet, Coutard, Ferte, Gautron, Gorbalenya, Heresanu, de Lamballerie, Lantez, Norder, Papageorgiou, Veesler
Collection: Acta Crystallogr. Sect. D-Biol. Crystallogr.
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Résumé     
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.
Added by: Laurent Cournède  
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