PMID:21821878

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Citation

Yamashita, E, Nakagawa, A, Takahashi, J, Tsunoda, K, Yamada, S and Takeda, S (2011) The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:837-41

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.

Links

PubMed PMC3151111 Online version:10.1107/S1744309111005999

Keywords

Amino Acid Sequence; Bacteriophage P2/chemistry; Bacteriophage P2/metabolism; Crystallography, X-Ray; Escherichia coli/chemistry; Iron/chemistry; Models, Molecular; Protein Binding; Protein Structure, Quaternary; Viral Tail Proteins/chemistry; Viral Tail Proteins/metabolism

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