2QQP

Crystal Structure of Authentic Providence Virus

Summary for 2QQP

• Entry DOI: 10.2210/pdb2qqp/pdb
• Descriptor: p81, RNA (5'-R(*UP*UP*UP*U)-3'), CALCIUM ION, ... (5 entities in total)
• Functional Keywords: virus, capsid, coat protein, protein-rna complex, beta barrel, ig-like domain, tetravirus, tetraviridae, icosahedral virus, quasiequivalence, auto-catalytic cleavage, auto proteolysis
• Biological source: Providence virus; More
• Total number of polymer chains: 9
• Total formula weight: 273836.65

Authors

Speir, J.A.,Taylor, D.J.,Johnson, J.E. (deposition date: 2007-07-26, release date: 2009-01-20, Last modification date: 2024-02-21)

Primary citation

Speir, J.A.,Taylor, D.J.,Natarajan, P.,Pringle, F.M.,Ball, L.A.,Johnson, J.E.
Evolution in action: N and C termini of subunits in related T = 4 viruses exchange roles as molecular switches.
Structure, 18:700-709, 2010

PubMed 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.

PubMed: 20541507
DOI: 10.1016/j.str.2010.03.010

Experimental method

X-RAY DIFFRACTION (3.8 Å)