3AQJ
Crystal Structure of a C-terminal domain of the bacteriophage P2 tail spike protein, gpV
Summary for 3AQJ
| Entry DOI | 10.2210/pdb3aqj/pdb |
| Descriptor | Baseplate assembly protein V, FE (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | bacteriophage, tail spike, iron binding, beta-helix, infection, metal binding protein |
| Biological source | Enterobacteria phage P2 (Bacteriophage P2) |
| Total number of polymer chains | 6 |
| Total formula weight | 84007.81 |
| Authors | Takeda, S.,Yamashita, E.,Nakagawa, A. (deposition date: 2010-11-06, release date: 2011-08-10, Last modification date: 2024-03-13) |
| Primary citation | 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 Cited by 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: 21821878DOI: 10.1107/S1744309111005999 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.27 Å) |
Structure validation
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