2VF9

Crystal structure of bacteriophage PRR1

2VF9 の概要

• エントリーDOI: 10.2210/pdb2vf9/pdb
• 分子名称: COAT PROTEIN, CALCIUM ION (2 entities in total)
• 機能のキーワード: virion, rna-binding, capsid protein, structural protein, virus
• 由来する生物種: BACTERIOPHAGE PRR1
• 細胞内の位置: Virion (Potential): P03616
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43745.58

構造登録者

Persson, M.,Tars, K.,Liljas, L. (登録日: 2007-11-01, 公開日: 2008-09-23, 最終更新日: 2023-12-13)

主引用文献

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

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: 18786545
DOI: 10.1016/J.JMB.2008.08.060

実験手法

X-RAY DIFFRACTION (3.5 Å)