3CJI

Structure of Seneca Valley Virus-001

Summary for 3CJI

• Entry DOI: 10.2210/pdb3cji/pdb
• Descriptor: Polyprotein, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: virus capsid protein structure, atp-binding, cytoplasm, cytoplasmic vesicle, helicase, hydrolase, membrane, nucleotide-binding, nucleotidyltransferase, phosphoprotein, protease, rna replication, rna-binding, rna-directed rna polymerase, thiol protease, transferase, virion, icosahedral virus, virus
• Biological source: Seneca valley virus; More
• Total number of polymer chains: 4
• Total formula weight: 94750.95

Authors

Venkataraman, S.,Reddy, V.S. (deposition date: 2008-03-13, release date: 2008-12-16, Last modification date: 2023-08-30)

Primary citation

Venkataraman, S.,Reddy, S.P.,Loo, J.,Idamakanti, N.,Hallenbeck, P.L.,Reddy, V.S.
Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus
Structure, 16:1555-1561, 2008

PubMed Abstract: The crystal structure of Seneca Valley Virus-001 (SVV-001), the representative member of a new genus, Senecavirus, is reported at 2.3A resolution. SVV-001 is the first naturally occurring nonpathogenic picornavirus shown to mediate selective cytotoxicity towards tumor cells with neuroendocrine cancer features. The nonsegmented (+) ssRNA genome of SVV-001 shares closest sequence similarity with the genomes of the members of Cardiovirus. The overall tertiary structure of VP1-VP4 subunits is conserved with the exception of loops, especially those of VP1 that show large deviations relative to the members of the cardioviruses. The surface loops of VP1 and VP2 are predicted to mediate cell tropism of SVV-001. In addition, the organization of the packaged nucleic acid density indicates that certain regions of VP2 and VP4 interact closely with the packaged nucleic acid.

PubMed: 18940610
DOI: 10.1016/j.str.2008.07.013

Experimental method

X-RAY DIFFRACTION (2.3 Å)