3J2M

The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the extended T4 tail

3J2M の概要

• エントリーDOI: 10.2210/pdb3j2m/pdb
• 関連するPDBエントリー: 3J2N 3J2O
• EMDBエントリー: 1126
• 分子名称: Tail connector protein Gp15, Tail sheath protein Gp18 (2 entities in total)
• 機能のキーワード: bacteriophage t4, phage tail terminator protein, phage sheath protein, viral protein
• 由来する生物種: Enterobacteria phage T4; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 617261.82

構造登録者

Fokine, A.,Zhang, Z.,Kanamaru, S.,Bowman, V.D.,Aksyuk, A.,Arisaka, F.,Rao, V.B.,Rossmann, M.G. (登録日: 2012-11-09, 公開日: 2013-03-06, 最終更新日: 2024-02-21)

主引用文献

Fokine, A.,Zhang, Z.,Kanamaru, S.,Bowman, V.D.,Aksyuk, A.A.,Arisaka, F.,Rao, V.B.,Rossmann, M.G.
The molecular architecture of the bacteriophage t4 neck.
J.Mol.Biol., 425:1731-1744, 2013

PubMed Abstract: A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers.

PubMed: 23434847
DOI: 10.1016/j.jmb.2013.02.012

実験手法

ELECTRON MICROSCOPY (15 Å)