SNAP output for PDB entry 5odv [SNAP web server]

PDB-id

5odv; SNAP-derived features in text and JSON formats; DNAproDB

Class

virus

Method

cryo-EM (4.0 Å)

Summary

Structure of watermelon mosaic virus potyvirus.

Reference

Zamora M, Mendez-Lopez E, Agirrezabala X, Cuesta R, Lavin JL, Sanchez-Pina MA, Aranda MA, Valle M (2017): "Potyvirus virion structure shows conserved protein fold and RNA binding site in ssRNA viruses." Sci Adv, 3, eaao2182. doi: 10.1126/sciadv.aao2182.

Abstract

Potyviruses constitute the second largest genus of plant viruses and cause important economic losses in a large variety of crops; however, the atomic structure of their particles remains unknown. Infective potyvirus virions are long flexuous filaments where coat protein (CP) subunits assemble in helical mode bound to a monopartite positive-sense single-stranded RNA [(+)ssRNA] genome. We present the cryo-electron microscopy (cryoEM) structure of the potyvirus watermelon mosaic virus at a resolution of 4.0 Å. The atomic model shows a conserved fold for the CPs of flexible filamentous plant viruses, including a universally conserved RNA binding pocket, which is a potential target for antiviral compounds. This conserved fold of the CP is widely distributed in eukaryotic viruses and is also shared by nucleoproteins of enveloped viruses with segmented (-)ssRNA (negative-sense ssRNA) genomes, including influenza viruses.