2X53

Structure of the phage p2 baseplate in its activated conformation with Sr

2X53 の概要

• エントリーDOI: 10.2210/pdb2x53/pdb
• 関連するPDBエントリー: 2WZP 2X54 2X5A
• EMDBエントリー: 1699
• 分子名称: ORF16, PUTATIVE RECEPTOR BINDING PROTEIN, ORF15, ... (4 entities in total)
• 機能のキーワード: baseplate, viral protein
• 由来する生物種: LACTOCOCCUS PHAGE P2 (PHAGE P2); 詳細
• タンパク質・核酸の鎖数: 27
• 化学式量合計: 849424.02

構造登録者

Sciara, G.,Bebeacua, C.,Bron, P.,Tremblay, D.,Ortiz-Lombardia, M.,Lichiere, J.,van Heel, M.,Campanacci, V.,Moineau, S.,Cambillau, C. (登録日: 2010-02-05, 公開日: 2010-02-16, 最終更新日: 2023-12-20)

主引用文献

Sciara, G.,Bebeacua, C.,Bron, P.,Tremblay, D.,Ortiz-Lombardia, M.,Lichiere, J.,van Heel, M.,Campanacci, V.,Moineau, S.,Cambillau, C.
Structure of Lactococcal Phage P2 Baseplate and its Mechanism of Activation.
Proc.Natl.Acad.Sci.USA, 107:6852-, 2010

PubMed Abstract: Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.

PubMed: 20351260
DOI: 10.1073/PNAS.1000232107

実験手法

X-RAY DIFFRACTION (3.9 Å)