3FOH

Fitting of gp18M crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 extended tail

3FOH の概要

• エントリーDOI: 10.2210/pdb3foh/pdb
• 関連するPDBエントリー: 3FO8 3FOA 3FOI
• EMDBエントリー: 1126
• 分子名称: Tail sheath protein Gp18 (1 entity in total)
• 機能のキーワード: alpha-beta, viral structural protein, bacteriophage t4, tail sheath, viral protein
• 由来する生物種: Enterobacteria phage T4 (Bacteriophage T4)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 327875.79

構造登録者

Aksyuk, A.A.,Leiman, P.G.,Kurochkina, L.P.,Shneider, M.M.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G. (登録日: 2008-12-30, 公開日: 2009-03-10, 最終更新日: 2024-02-21)

主引用文献

Aksyuk, A.A.,Leiman, P.G.,Kurochkina, L.P.,Shneider, M.M.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G.
The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria.
Embo J., 28:821-829, 2009

PubMed Abstract: The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central non-contractile tail tube. The contraction of the sheath drives the tail tube through the outer membrane, creating a channel for the viral genome delivery. A crystal structure of about three quarters of gp18 has been determined and was fitted into cryo-electron microscopy reconstructions of the tail sheath before and after contraction. It was shown that during contraction, gp18 subunits slide over each other with no apparent change in their structure.

PubMed: 19229296
DOI: 10.1038/emboj.2009.36

実験手法

ELECTRON MICROSCOPY (15 Å)