3AQJ

Crystal Structure of a C-terminal domain of the bacteriophage P2 tail spike protein, gpV

3AQJ の概要

• エントリーDOI: 10.2210/pdb3aqj/pdb
• 分子名称: Baseplate assembly protein V, FE (II) ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: bacteriophage, tail spike, iron binding, beta-helix, infection, metal binding protein
• 由来する生物種: Enterobacteria phage P2 (Bacteriophage P2)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 84007.81

構造登録者

Takeda, S.,Yamashita, E.,Nakagawa, A. (登録日: 2010-11-06, 公開日: 2011-08-10, 最終更新日: 2024-03-13)

主引用文献

Yamashita, E.,Nakagawa, A.,Takahashi, J.,Tsunoda, K.,Yamada, S.,Takeda, S.
The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure
Acta Crystallogr.,Sect.F, 67:837-841, 2011

PubMed Abstract: The adsorption and infection of bacteriophage P2 is mediated by tail fibres and tail spikes. The tail spikes on the tail baseplate are used to irreversibly adsorb to the host cells. Recently, a P2 phage tail-spike protein, gpV, was purified and it was shown that a C-terminal domain, Ser87-Leu211, is sufficient for the binding of gpV to host Escherichia coli membranes [Kageyama et al. (2009), Biochemistry, 48, 10129-10135]. In this paper, the crystal structure of the C-terminal domain of P2 gpV is reported. The structure is a triangular pyramid and looks like a spearhead composed of an intertwined β-sheet, a triple β-helix and a metal-binding region containing iron, calcium and chloride ions.

PubMed: 21821878
DOI: 10.1107/S1744309111005999

実験手法

X-RAY DIFFRACTION (1.27 Å)