7OZ4

Mature capsid of bacteriophage phiRSA1

7OZ4 の概要

• エントリーDOI: 10.2210/pdb7oz4/pdb
• EMDBエントリー: 13120
• 分子名称: p2 family phage major capsid protein (1 entity in total)
• 機能のキーワード: bacteriophage, capsid, virus
• 由来する生物種: Ralstonia virus RSA1
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 264820.72

構造登録者

Effantin, G.,Fujiwara, A.,Kawsaki, T.,Yamada, T.,Schoehn, G. (登録日: 2021-06-25, 公開日: 2021-11-17, 最終更新日: 2024-07-17)

主引用文献

Effantin, G.,Fujiwara, A.,Kawasaki, T.,Yamada, T.,Schoehn, G.
High Resolution Structure of the Mature Capsid of Ralstonia solanacearum Bacteriophage phi RSA1 by Cryo-Electron Microscopy.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: The ϕRSA1 bacteriophage has been isolated from , a gram negative bacteria having a significant economic impact on many important crops. We solved the three-dimensional structure of the ϕRSA1 mature capsid to 3.9 Å resolution by cryo-electron microscopy. The capsid shell, that contains the 39 kbp of dsDNA genome, has an icosahedral symmetry characterized by an unusual triangulation number of T = 7, . The ϕRSA1 capsid is composed solely of the polymerization of the major capsid protein, gp8, which exhibits the typical "Johnson" fold first characterized in bacteriophage HK97. As opposed to the latter, the ϕRSA1 mature capsid is not stabilized by covalent crosslinking between its subunits, nor by the addition of a decoration protein. We further describe the molecular interactions occurring between the subunits of the ϕRSA1 capsid and their relationships with the other known bacteriophages.

PubMed: 34681713
DOI: 10.3390/ijms222011053

実験手法

ELECTRON MICROSCOPY (3.9 Å)