4EO2

Structure of the bacteriophage C1 tail knob protein, gp12

4EO2 の概要

• エントリーDOI: 10.2210/pdb4eo2/pdb
• 関連するPDBエントリー: 4EP0
• 分子名称: Major tail protein (1 entity in total)
• 機能のキーワード: structural protein, viral protein
• 由来する生物種: Streptococcus phage C1
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 400930.78

構造登録者

Aksyuk, A.A.,Rossmann, M.G. (登録日: 2012-04-13, 公開日: 2012-08-22, 最終更新日: 2024-02-28)

主引用文献

Aksyuk, A.A.,Bowman, V.D.,Kaufmann, B.,Fields, C.,Klose, T.,Holdaway, H.A.,Fischetti, V.A.,Rossmann, M.G.
Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry.
Proc.Natl.Acad.Sci.USA, 109:14001-14006, 2012

PubMed Abstract: The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a ϕ29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.

PubMed: 22891295
DOI: 10.1073/pnas.1207730109

実験手法

X-RAY DIFFRACTION (3.007 Å)