ArticleStructure (London, England : 1993)2010
Evolution in action: N and C termini of subunits in related T = 4 viruses exchange roles as molecular switches.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling.Virology journal · 2025Article
- Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.Journal of virology · 2025Article
- Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions.Nature communications · 2023Article
- Article
- Molecular and biochemical characterization of the NS1 protein of non-cultured influenza B virus strains circulating in Singapore.Microbial genomics · 2016Article
- Assembly and maturation of a T = 4 quasi-equivalent virus is guided by electrostatic and mechanical forces.Viruses · 2014Review
- Identification and characterization of RNA duplex unwinding and ATPase activities of an alphatetravirus superfamily 1 helicase.Virology · 2012Article
- Dissecting quasi-equivalence in nonenveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers.Journal of virology · 2012Article
- Nucleic acid packaging in viruses.Current opinion in structural biology · 2012Review
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Authors and funding
6 authors.
Funding
Abstract
The T = 4 tetravirus and T = 3 nodavirus capsid proteins undergo closely similar autoproteolysis to produce the N-terminal beta and C-terminal, lipophilic gamma polypeptides. The gamma peptides and the N termini of beta also act as molecular switches that determine their quasi equivalent capsid structures. The crystal structure of Providence virus (PrV), only the second of a tetravirus (the first was NomegaV), reveals conserved folds and cleavage sites, but the protein termini have completely different structures and the opposite functions of those in NomegaV. N termini of beta form the molecular switch in PrV, whereas gamma peptides play this role in NomegaV. PrV gamma peptides instead interact with packaged RNA at the particle two-folds by using a repeating sequence pattern found in only four other RNA- or membrane-binding proteins. The disposition of peptide termini in PrV is closely related to those in nodaviruses, suggesting that PrV may be closer to the primordial T = 4 particle than NomegaV.
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