2BSG

The modeled structure of fibritin (gpwac) of bacteriophage T4 based on cryo-EM reconstruction of the extended tail of bacteriophage T4

2BSG の概要

• エントリーDOI: 10.2210/pdb2bsg/pdb
• 関連するPDBエントリー: 1AA0 1AVY 1OX3 1RFO 1V1H 1V1I
• EMDBエントリー: 1126
• 分子名称: FIBRITIN (1 entity in total)
• 機能のキーワード: viral protein, attachment protein, bacteriophage assembly, bacteriophage t4, chaperone, fibritin, structural protein
• 由来する生物種: BACTERIOPHAGE T4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 155727.49

構造登録者

Kostyuchenko, V.A.,Chipman, P.R.,Leiman, P.G.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G. (登録日: 2005-05-20, 公開日: 2005-09-21, 最終更新日: 2024-05-08)

主引用文献

Kostyuchenko, V.A.,Chipman, P.R.,Leiman, P.G.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G.
The Tail Structure of Bacteriophage T4 and its Mechanism of Contraction.
Nat.Struct.Mol.Biol., 12:810-, 2005

PubMed Abstract: Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space.

PubMed: 16116440
DOI: 10.1038/NSMB975

実験手法

ELECTRON MICROSCOPY (15 Å)