P2噬菌体尾刺的宿主结合结构域揭示了一种三聚体铁结合结构。
The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure.
作者信息
Yamashita Eiki, Nakagawa Atsushi, Takahashi Junichi, Tsunoda Kin-ichi, Yamada Seiko, Takeda Shigeki
机构信息
Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):837-41. doi: 10.1107/S1744309111005999. Epub 2011 Jul 13.
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.
摘要
噬菌体P2的吸附和感染由尾丝和尾刺介导。尾基板上的尾刺用于不可逆地吸附宿主细胞。最近，一种P2噬菌体尾刺蛋白gpV被纯化，结果表明其C末端结构域（Ser87-Leu211）足以使gpV与宿主大肠杆菌膜结合[Kageyama等人（2009年），《生物化学》，48卷，10129 - 10135页]。本文报道了P2 gpV C末端结构域的晶体结构。该结构为三角锥，看起来像一个由相互缠绕的β折叠、三重β螺旋以及包含铁、钙和氯离子的金属结合区域组成的矛头。
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