9JYY

core proteins of mature T7

9JYY の概要

• エントリーDOI: 10.2210/pdb9jyy/pdb
• EMDBエントリー: 61909
• 分子名称: Protein 6.7, Internal virion protein gp14, Internal virion protein gp15, ... (4 entities in total)
• 機能のキーワード: complex, viral protein
• 由来する生物種: Escherichia phage T7; 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 1494507.77

構造登録者

Liu, H.R.,Chen, W.Y. (登録日: 2024-10-13, 公開日: 2024-12-11, 最終更新日: 2025-06-25)

主引用文献

Zheng, J.,Xiao, H.,Pang, H.,Wang, L.,Song, J.,Chen, W.,Cheng, L.,Liu, H.
Conformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages.
J.Virol., 99:e0124924-e0124924, 2025

PubMed Abstract: Podophage tails are too short to span the cell envelope during infection. Consequently, podophages initially eject the core proteins within the head for the formation of an elongated trans-envelope channel for DNA ejection. Although the core proteins of bacteriophage T7 have been resolved at near-atomic resolution, the mechanisms of core proteins and DNA ejection remain to be fully elucidated. In this study, we provided improved structures of core proteins in mature T7 and the portal-tail complex in lipopolysaccharide-induced DNA-ejected T7 to resolutions of approximately 3 Å. Using these structures, we identified three small proteins, namely gp14, gp6.7, and gp7.3, and illustrated the conformational changes in and translocation of these proteins from the mature to DNA-ejected states. Our structures indicate that gp6.7, which participates in the assembly of the core and trans-envelope channel, is a core protein, and that gp7.3 serves as a structural scaffold to assist the assembly of the nozzle into the adaptor.

PubMed: 39704524
DOI: 10.1128/jvi.01249-24

実験手法

ELECTRON MICROSCOPY (3 Å)