3H3Y

Fitting of the gp6 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 star-shaped baseplate

3H3Y の概要

• エントリーDOI: 10.2210/pdb3h3y/pdb
• 関連するPDBエントリー: 3H2T 3H3W
• EMDBエントリー: 1086
• 分子名称: Baseplate structural protein Gp6 (1 entity in total)
• 機能のキーワード: viral structural protein, virion, viral protein
• 由来する生物種: bacteriophage T4
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 459653.39

構造登録者

Aksyuk, A.A.,Leiman, P.G.,Shneider, M.M.,Mesyanzhinov, V.V.,Rossmann, M.G. (登録日: 2009-04-17, 公開日: 2009-05-19, 最終更新日: 2024-02-21)

主引用文献

Aksyuk, A.A.,Leiman, P.G.,Shneider, M.M.,Mesyanzhinov, V.V.,Rossmann, M.G.
The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate.
Structure, 17:800-808, 2009

PubMed Abstract: The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring.

PubMed: 19523898
DOI: 10.1016/j.str.2009.04.005

実験手法

ELECTRON MICROSCOPY (16 Å)