2VF9
Crystal structure of bacteriophage PRR1
Summary for 2VF9
| Entry DOI | 10.2210/pdb2vf9/pdb |
| Descriptor | COAT PROTEIN, CALCIUM ION (2 entities in total) |
| Functional Keywords | virion, rna-binding, capsid protein, structural protein, virus |
| Biological source | BACTERIOPHAGE PRR1 |
| Cellular location | Virion (Potential): P03616 |
| Total number of polymer chains | 3 |
| Total formula weight | 43745.58 |
| Authors | Persson, M.,Tars, K.,Liljas, L. (deposition date: 2007-11-01, release date: 2008-09-23, Last modification date: 2023-12-13) |
| Primary citation | Persson, M.,Tars, K.,Liljas, L. The Capsid of the Small RNA Phage Prr1 is Stabilized by Metal Ions J.Mol.Biol., 383:914-, 2008 Cited by PubMed 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. PubMed: 18786545DOI: 10.1016/J.JMB.2008.08.060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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