title: The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure.
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.
authors.affiliation: Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
authors.forename: Eiki
authors.initials: E
authors.lastname: Yamashita
authors.forename: Atsushi
authors.initials: A
authors.lastname: Nakagawa
authors.forename: Junichi
authors.initials: J
authors.lastname: Takahashi
authors.forename: Kin-ichi
authors.initials: K
authors.lastname: Tsunoda
authors.forename: Seiko
authors.initials: S
authors.lastname: Yamada
authors.forename: Shigeki
authors.initials: S
authors.lastname: Takeda
mesh_terms: D000595:Amino Acid Sequence; D017901:Bacteriophage P2 / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D006026:Glycoside Hydrolases; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D017376:Viral Tail Proteins; D007501:Iron; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage