2FSY

Bacteriophage HK97 Pepsin-treated Expansion Intermediate IV

2FSY の概要

• エントリーDOI: 10.2210/pdb2fsy/pdb
• 関連するPDBエントリー: 2FRP 2FS3 2FT1 2FTE
• 分子名称: major capsid protein (1 entity in total)
• 機能のキーワード: bacteriophage, hk97, capsid protein, expansion intermediate, icosahedral virus, virus
• 由来する生物種: Enterobacteria phage HK97
• 細胞内の位置: Virion: P49861
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 215632.25

構造登録者

Gan, L.,Speir, J.A.,Conway, J.F.,Lander, G.,Cheng, N.,Firek, B.A.,Hendrix, R.W.,Duda, R.L.,Liljas, L.,Johnson, J.E. (登録日: 2006-01-23, 公開日: 2006-02-07, 最終更新日: 2023-09-20)

主引用文献

Gan, L.,Speir, J.A.,Conway, J.F.,Lander, G.,Cheng, N.,Firek, B.A.,Hendrix, R.W.,Duda, R.L.,Liljas, L.,Johnson, J.E.
Capsid Conformational Sampling in HK97 Maturation Visualized by X-Ray Crystallography and Cryo-EM.
Structure, 14:1655-1665, 2006

PubMed Abstract: Maturation of the bacteriophage HK97 capsid from a precursor (Prohead II) to the mature state (Head II) involves a 60 A radial expansion. The mature particle is formed by 420 copies of the major capsid protein organized on a T = 7 laevo lattice with each subunit covalently crosslinked to two neighbors. Well-characterized pH 4 expansion intermediates make HK97 valuable for investigating quaternary structural dynamics. Here, we use X-ray crystallography and cryo-EM to demonstrate that in the final transition in maturation (requiring neutral pH), pentons in Expansion Intermediate IV (EI-IV) reversibly sample 14 A translations and 6 degrees rotations relative to a fixed hexon lattice. The limit of this trajectory corresponds to the Head II conformation that is secured at this extent only by the formation of the final class of covalent crosslinks. Mutants that cannot crosslink or EI-IV particles that have been rendered incapable of forming the final crosslink remain in the EI-IV state.

PubMed: 17098191
DOI: 10.1016/j.str.2006.09.006

実験手法

X-RAY DIFFRACTION (3.8 Å)