9IMH

Structure of urea-treated empty bacteriophage T5 connector complex

9IMH の概要

• エントリーDOI: 10.2210/pdb9imh/pdb
• EMDBエントリー: 60689
• 分子名称: Tail tube terminator protein p142 (1 entity in total)
• 機能のキーワード: complex, viral protein
• 由来する生物種: Escherichia phage T5
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 110271.86

構造登録者

Peng, Y.N.,Liu, H.R. (登録日: 2024-07-03, 公開日: 2024-10-02)

主引用文献

Peng, Y.,Tang, H.,Xiao, H.,Chen, W.,Song, J.,Zheng, J.,Liu, H.
Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection.
Int J Mol Sci, 25:-, 2024

PubMed Abstract: T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, we used cryo-electron microscopy (cryo-EM) to determine the structures of mature T5 (a laboratory-adapted, fiberless T5 mutant) and urea-treated empty T5 (lacking the tip complex) at near-atomic resolutions. Atomic models of the head, connector complex, tail tube, and tail tip were built for mature T5, and atomic models of the connector complex, comprising the portal protein pb7, adaptor protein p144, and tail terminator protein p142, were built for urea-treated empty T5. Our findings revealed that the aforementioned proteins did not undergo global conformational changes before and after DNA ejection, indicating that these structural features were conserved among most myophages and siphophages. The present study elucidates the underlying mechanisms of siphophage infection and DNA ejection.

PubMed: 39126049
DOI: 10.3390/ijms25158479

実験手法

ELECTRON MICROSCOPY (4.2 Å)