The capsid of the small RNA phage PRR1 is stabilized by metal ions.
2008 (English)In: Journal of molecular biology, ISSN 1089-8638, Vol. 383, no 4, 914-22 p.Article in journal (Refereed) Published
Many nonenveloped virus particles are stabilized by calcium ions bound in the interfaces between the protein subunits. These ions may have a role in the disassembly process. The small RNA phages of the Leviviridae family have T=3 quasi-symmetry and are unique among simple viruses in that they have a coat protein with a translational repressor activity and a fold that has not been observed in other viruses. The crystal structure of phage PRR1 has been determined to 3.5 A resolution. The structure shows a tentative binding site for a calcium ion close to the quasi-3-fold axis. The RNA-binding surface used for repressor activity is mostly conserved. The structure does not show any significant differences between quasi-equivalent subunits, which suggests that the assembly is not controlled by conformational switches as in many other simple viruses.
Place, publisher, year, edition, pages
2008. Vol. 383, no 4, 914-22 p.
IdentifiersURN: urn:nbn:se:uu:diva-104176DOI: 10.1016/j.jmb.2008.08.060ISI: 000260533800015PubMedID: 18786545OAI: oai:DiVA.org:uu-104176DiVA: diva2:219445