8FQK

Asymmetric unit of HK97 phage prohead I

8FQK の概要

• エントリーDOI: 10.2210/pdb8fqk/pdb
• 関連するPDBエントリー: 3e8k 3qpr
• EMDBエントリー: 29390
• 分子名称: Scaffolding domain delta (1 entity in total)
• 機能のキーワード: prohead i, icosahedral symmetry, hk97, phage, capsid, virus
• 由来する生物種: Escherichia phage HK97
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 296005.17

構造登録者

Huet, A.,Oh, B.,Maurer, J.,Duda, R.L.,Conway, J.F. (登録日: 2023-01-06, 公開日: 2023-06-28, 最終更新日: 2024-06-19)

主引用文献

Huet, A.,Oh, B.,Maurer, J.,Duda, R.L.,Conway, J.F.
A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.
Sci Adv, 9:eadg8868-eadg8868, 2023

PubMed Abstract: Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have determined the portal vertex structure of the bacteriophage HK97 procapsid, where the scaffold is a domain of the major capsid protein. The scaffold forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and is further stabilized around the portal, forming trimeric coiled-coil towers, two per surrounding capsomer. These 10 towers bind identically to 10 of 12 portal subunits, adopting a pseudo-12-fold organization that explains how the symmetry mismatch is managed at this early step.

PubMed: 37327331
DOI: 10.1126/sciadv.adg8868

実験手法

ELECTRON MICROSCOPY (3.5 Å)