7RWZ

SaPIbov5 procapsid structure including size redirecting protein Ccm

7RWZ の概要

• エントリーDOI: 10.2210/pdb7rwz/pdb
• EMDBエントリー: 24720
• 分子名称: Cos capsid morphogenesis protein (Ccm), Major capsid protein (2 entities in total)
• 機能のキーワード: hk97-like fold, capsid size redirection, major capsid protein, virus
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 176346.56

構造登録者

Hawkins, N.C.,Kizziah, J.L.,Dokland, T. (登録日: 2021-08-20, 公開日: 2021-11-17, 最終更新日: 2025-05-28)

主引用文献

Hawkins, N.C.,Kizziah, J.L.,Penades, J.R.,Dokland, T.
Shape shifter: redirection of prolate phage capsid assembly by staphylococcal pathogenicity islands.
Nat Commun, 12:6408-6408, 2021

PubMed Abstract: Staphylococcus aureus pathogenicity islands (SaPIs) are molecular parasites that hijack helper phages for their transfer. SaPIbov5, the prototypical member of a family of cos type SaPIs, redirects the assembly of ϕ12 helper capsids from prolate to isometric. This size and shape shift is dependent on the SaPIbov5-encoded protein Ccm, a homolog of the ϕ12 capsid protein (CP). Using cryo-electron microscopy, we have determined structures of prolate ϕ12 procapsids and isometric SaPIbov5 procapsids. ϕ12 procapsids have icosahedral end caps with T = 4 architecture and a T = 14 cylindrical midsection, whereas SaPIbov5 procapsids have T = 4 icosahedral architecture. We built atomic models for CP and Ccm, and show that Ccm occupies the pentameric capsomers in the isometric SaPIbov5 procapsids, suggesting that preferential incorporation of Ccm pentamers prevents the cylindrical midsection from forming. Our results highlight that pirate elements have evolved diverse mechanisms to suppress phage multiplication, including the acquisition of phage capsid protein homologs.

PubMed: 34737316
DOI: 10.1038/s41467-021-26759-x

実験手法

ELECTRON MICROSCOPY (4 Å)