5ODV

Structure of Watermelon mosaic virus potyvirus.

Summary for 5ODV

• Entry DOI: 10.2210/pdb5odv/pdb
• EMDB information: 3785
• Descriptor: coat protein, RNA (5'-R(P*UP*UP*UP*UP*U)-3') (2 entities in total)
• Functional Keywords: filamentous virus, potyvirus, plant pathogen, virus
• Biological source: Watermelon mosaic virus; More
• Total number of polymer chains: 48
• Total formula weight: 790782.82

Authors

Zamora, M.,Mendez-Lopez, E.,Agirrezabala, X.,Cuesta, R.,Lavin, J.L.,Sanchez-Pina, M.A.,Aranda, M.,Valle, M. (deposition date: 2017-07-06, release date: 2017-09-27, Last modification date: 2024-05-15)

Primary citation

Zamora, M.,Mendez-Lopez, E.,Agirrezabala, X.,Cuesta, R.,Lavin, J.L.,Sanchez-Pina, M.A.,Aranda, M.A.,Valle, M.
Potyvirus virion structure shows conserved protein fold and RNA binding site in ssRNA viruses.
Sci Adv, 3:eaao2182-eaao2182, 2017

PubMed 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.

PubMed: 28948231
DOI: 10.1126/sciadv.aao2182

Experimental method

ELECTRON MICROSCOPY (4 Å)