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TitleCryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses.
Journal, issue, pagesJ Virol, Vol. 86, Issue 15, Page 8314-8318, Year 2012
Publish dateMay 16, 2012
AuthorsJosué Gómez-Blanco / Daniel Luque / José M González / José L Carrascosa / Carlos Alfonso / Benes Trus / Wendy M Havens / Said A Ghabrial / José R Castón /
PubMed AbstractCryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical ...Cryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical core, indicative of gene duplication. This unusual organization is common to chrysoviruses. The arrangement of many of these putative α-helices is conserved in the totivirus L-A capsid protein, suggesting a shared motif. Our results indicate that a 120-subunit T=1 capsid is a conserved architecture that optimizes dsRNA replication and organization.
External linksJ Virol / PubMed:22593169 / PubMed Central
MethodsEM (single particle)
Resolution8.1 Å
Structure data

EMDB-2062:
Cryphonectria nitschkei Virus (CnV)capsid
Method: EM (single particle) / Resolution: 8.1 Å

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