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-Structure paper
タイトル | Cryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses. |
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ジャーナル・号・ページ | J Virol, Vol. 86, Issue 15, Page 8314-8318, Year 2012 |
掲載日 | 2012年5月16日 |
著者 | Josué Gómez-Blanco / Daniel Luque / José M González / José L Carrascosa / Carlos Alfonso / Benes Trus / Wendy M Havens / Said A Ghabrial / José R Castón / |
PubMed 要旨 | 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 ...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. |
リンク | J Virol / PubMed:22593169 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 8.1 Å |
構造データ | EMDB-2062: |