Evolution in Action: N and C Termini of Subunits in Related T = 4 Viruses Exchange Roles as Molecular Switches
| Autor: | Padmaja Natarajan, L. Andrew Ball, Jeffrey A. Speir, Derek James Taylor, John E. Johnson, Fiona M. Pringle |
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| Rok vydání: | 2010 |
| Předmět: |
EVO_ECOL
MICROBIO PROTEINS Stereochemistry viruses Peptide Biology Cleavage (embryo) Article Virus Sequence pattern Capsid Structural Biology RNA Viruses Molecular Biology Molecular switch chemistry.chemical_classification Base Sequence RNA biochemical phenomena metabolism and nutrition Biological Evolution Molecular biology chemistry Viruses Providence virus Capsid Proteins |
| Zdroj: | Structure. 18(6):700-709 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2010.03.010 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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