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Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1116-20. doi: 10.1107/S090744491002809X. Epub 2010 Sep 18.

The 2C putative helicase of echovirus 30 adopts a hexameric ring-shaped structure.

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Architecture et Fonction des Macromolécules Biologiques, UMR 6098 Centre National de la Recherche Scientifique, Université de la Méditerranée and Université de Provence, Case 925, 163 Avenue de Luminy, 13288 Marseille CEDEX 9, France.


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 ∼12 nm external diameter. Image analysis revealed that these particles were hexameric and resembled those formed by superfamily 3 DNA virus helicases.

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