3QR7

Crystal structure of the C-terminal fragment of the bacteriophage P2 membrane-piercing protein gpV

3QR7 の概要

• エントリーDOI: 10.2210/pdb3qr7/pdb
• 関連するPDBエントリー: 3QR8
• 分子名称: Baseplate assembly protein V, CHLORIDE ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: beta-helix, ob-fold, phage baseplate, iron-binding, cell membrane piercing, tail spike, viral protein
• 由来する生物種: Enterobacteria phage P2 (Bacteriophage P2)
• 細胞内の位置: Virion : P31340
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23872.19

構造登録者

Browning, C.,Shneider, M.,Leiman, P.G. (登録日: 2011-02-17, 公開日: 2012-02-22, 最終更新日: 2024-02-21)

主引用文献

Browning, C.,Shneider, M.M.,Bowman, V.D.,Schwarzer, D.,Leiman, P.G.
Phage pierces the host cell membrane with the iron-loaded spike.
Structure, 20:326-339, 2012

PubMed Abstract: Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and ϕ92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10Å diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.

PubMed: 22325780
DOI: 10.1016/j.str.2011.12.009

実験手法

X-RAY DIFFRACTION (0.94 Å)