AI Article Synopsis
- The 2C protein from the Picornaviridae family is a highly conserved ATPase and a potential antiviral target, but its structure and function are not yet well understood.
- Researchers investigated a modified version of the 2C protein from echovirus 30 using various techniques, including microscopy and enzymatic assays.
- The study found that this protein forms ring-like structures approximately 12 nm in diameter that are hexameric and similar to those produced by certain DNA virus helicases.
Article Abstract
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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| http://dx.doi.org/10.1107/S090744491002809X | DOI Listing |
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