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

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...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2010-10, Vol.66 (10), p.1116-1120
Main Authors: Papageorgiou, Nicolas, Coutard, Bruno, Lantez, Violaine, Gautron, Eric, Chauvet, Olivier, Baronti, Cécile, Norder, Heléne, De Lamballerie, Xavier, Heresanu, Vasile, Ferté, Nathalie, Veesler, Stéphane, Gorbalenya, Alexander E., Canard, Bruno
Format: Article
Language:English
Subjects:
2C protein
DNA Viruses - physiology
Echovirus 30
Enterovirus B, Human - physiology
In Vitro Techniques
Microscopy, Atomic Force
Microscopy, Electron, Transmission
Picornaviridae
Protein Conformation
Protein Multimerization
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Recombinant Proteins - ultrastructure
RNA Helicases - chemistry
RNA Helicases - genetics
RNA Helicases - metabolism
RNA Helicases - ultrastructure
Structural Homology, Protein
transmission electron microscopy
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Viral Proteins - ultrastructure
Virion - chemistry
Virion - ultrastructure
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Summary: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.
ISSN:1399-0047
0907-4449
2059-7983
1399-0047
2059-7983
DOI:10.1107/S090744491002809X