4AN5

Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly

4AN5 の概要

• エントリーDOI: 10.2210/pdb4an5/pdb
• EMDBエントリー: 2049
• 分子名称: COAT PROTEIN (1 entity in total)
• 機能のキーワード: virus, bacteriophage capsid spp1
• 由来する生物種: BACILLUS PHAGE SPP1
• 細胞内の位置: Virion : Q38582
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 247727.35

構造登録者

White, H.E.,Sherman, M.B.,Brasiles, S.,Jacquet, E.,Seavers, P.,Tavares, P.,Orlova, E.V. (登録日: 2012-03-15, 公開日: 2012-08-29, 最終更新日: 2024-05-08)

主引用文献

White, H.E.,Sherman, M.B.,Brasiles, S.,Jacquet, E.,Seavers, P.,Tavares, P.,Orlova, E.V.
Capsid Structure and its Stability at the Late Stages of Bacteriophage Spp1 Assembly.
J.Virol., 86:6768-, 2012

PubMed Abstract: The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12, which are organized in a T=7 lattice. DNA is arranged in layers with a distance of ~24.5 Å. gp12 forms spikes that are anchored at the center of gp13 hexamers. In a gp12-deficient mutant, the centers of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudoatomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between the thermostability of the capsid and those of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle coevolved toward high robustness.

PubMed: 22514336
DOI: 10.1128/JVI.00412-12

実験手法

ELECTRON MICROSCOPY (8.8 Å)