The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure.
The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure.
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DOI：
10.1107/s1744309111005999
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发表时间：
2011-08
期刊：
影响因子：
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通讯作者：
E. Yamashita;A. Nakagawa;J. Takahashi;K. Tsunoda;S. Yamada;S. Takeda
中科院分区：
文献类型：
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作者：
E. Yamashita;A. Nakagawa;J. Takahashi;K. Tsunoda;S. Yamada;S. Takeda
噬菌体P2的吸附和感染是由尾纤维和尾刺介导的。尾基板上的尾刺用于不可逆地吸附至宿主细胞。最近，纯化了P2噬菌体尾刺蛋白gpV，并且显示C-末端结构域Ser 87-Leu 211足以使gpV结合宿主大肠杆菌膜[Kageyama等人（2009），Biochemistry，48，10129-10135]。本文报道了P2 gpV的C-末端结构域的晶体结构。该结构是一个三角金字塔，看起来像一个矛头，由一个相互缠绕的β-折叠，一个三重β-螺旋和一个含有铁，钙和氯离子的金属结合区组成。
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.