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Crystal Structure of Authentic Providence VirusCrystal Structure of Authentic Providence Virus
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Evolution in action: N and C termini of subunits in related T = 4 viruses exchange roles as molecular switches.,Speir JA, Taylor DJ, Natarajan P, Pringle FM, Ball LA, Johnson JE Structure. 2010 Jun 9;18(6):700-9. PMID:20541507[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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