3VTO

The crystal structure of the C-terminal domain of Mu phage central spike

3VTO の概要

• エントリーDOI: 10.2210/pdb3vto/pdb
• 関連するPDBエントリー: 3VTN
• 分子名称: Protein gp45, FE (III) ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: beta-helix, central spike, mu phage, metal binding protein
• 由来する生物種: Enterobacteria phage Mu
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 77352.88

構造登録者

Harada, K.,Yamashita, E.,Nakagawa, A.,Takeda, S. (登録日: 2012-06-01, 公開日: 2013-02-06, 最終更新日: 2024-03-20)

主引用文献

Harada, K.,Yamashita, E.,Nakagawa, A.,Miyafusa, T.,Tsumoto, K.,Ueno, T.,Toyama, Y.,Takeda, S.
Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion
Biochim.Biophys.Acta, 1834:284-291, 2013

PubMed Abstract: Bacteriophage Mu, which has a contractile tail, is one of the most famous genus of Myoviridae. It has a wide host range and is thought to contribute to horizontal gene transfer. The Myoviridae infection process is initiated by adhesion to the host surface. The phage then penetrates the host cell membrane using its tail to inject its genetic material into the host. In this penetration process, Myoviridae phages are proposed to puncture the membrane of the host cell using a central spike located beneath its baseplate. The central spike of the Mu phage is thought to be composed of gene 45 product (gp45), which has a significant sequence homology with the central spike of P2 phage (gpV). We determined the crystal structure of shortened Mu gp45Δ1-91 (Arg92-Gln197) at 1.5Å resolution and showed that Mu gp45 is a needlelike structure that punctures the membrane. The apex of Mu gp45 and that of P2 gpV contained iron, chloride, and calcium ions. Although the C-terminal domain of Mu gp45 was sufficient for binding to the E. coli membrane, a mutant D188A, in which the Asp amino acid residue that coordinates the calcium ion was replaced by Ala, did not exhibit a propensity to bind to the membrane. Therefore, we concluded that calcium ion played an important role in interaction with the host cell membrane.

PubMed: 22922659
DOI: 10.1016/j.bbapap.2012.08.015

実験手法

X-RAY DIFFRACTION (1.44 Å)