9E99

Cryo-EM reconstruction of Escherichia phage N4 capsid

9E99 の概要

• エントリーDOI: 10.2210/pdb9e99/pdb
• EMDBエントリー: 47777
• 分子名称: Major capsid protein, 32 kDa protein (2 entities in total)
• 機能のキーワード: bacteriophage, capsid, hoc-like decoration protein, ig-like decoration protein, schitoviridae, n4, enquatroviridae, viral protein
• 由来する生物種: Escherichia phage N4; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 484291.04

構造登録者

Eruera, A.,McJarrow-Keller, K.,Hyun, J.K.,Bostina, M. (登録日: 2024-11-07, 公開日: 2025-02-19)

主引用文献

McJarrow-Keller, K.,Eruera, A.R.,Crowe, A.J.M.,Kumaran, R.,Hyun, J.,Bostina, M.
Atlas of Interactions Between Decoration Proteins and Major Capsid Proteins of Coliphage N4.
Viruses, 17:-, 2024

PubMed Abstract: Coliphage N4 is a representative species of the family of bacteriophages. Originally structurally studied in 2008, the capsid structure was solved to 14 Å to reveal an interesting arrangement of Ig-like decoration proteins across the surface of the capsid. Herein, we present a high-resolution N4 structure, reporting a 2.45 Å map of the capsid obtained via single particle cryogenic-electron microscopy. Structural analysis of the major capsid proteins (MCPs) and decoration proteins (gp56 and gp17) of phage N4 reveals a pattern of interactions across the capsid that are mediated by structurally homologous domains of gp17. In this study, an analysis of the complex interface contacts allows us to confirm that the gp17 Ig-like decoration proteins of N4 are likely employed by the virus to increase the capsid's structural integrity.

PubMed: 39861808
DOI: 10.3390/v17010019

実験手法

ELECTRON MICROSCOPY (2.45 Å)