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• W2019427641 endingPage "922" @default.
• W2019427641 startingPage "914" @default.
• W2019427641 abstract "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." @default.
• W2019427641 created "2016-06-24" @default.
• W2019427641 creator A5024838105 @default.
• W2019427641 creator A5039310187 @default.
• W2019427641 creator A5080807999 @default.
• W2019427641 date "2008-11-01" @default.
• W2019427641 modified "2023-10-13" @default.
• W2019427641 title "The Capsid of the Small RNA Phage PRR1 Is Stabilized by Metal Ions" @default.
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• W2019427641 doi "https://doi.org/10.1016/j.jmb.2008.08.060" @default.
• W2019427641 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18786545" @default.
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