The capsid of the small RNA phage PRR1 is stabilized by metal ions |
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Authors: | Persson Magnus Tars Kaspars Liljas Lars |
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Affiliation: | Department of Cell and Molecular Biology, Uppsala University, BMC, Husargatan 3, Box 596, S-751 24 Uppsala, Sweden |
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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 Å 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. |
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Keywords: | EDTA, ethylenediaminetetraacetic acid PEG, polyethylene glycol PDB, Protein Data Bank |
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