9KHX

Neck structure of Escherichia phage Mu

9KHX の概要

• エントリーDOI: 10.2210/pdb9khx/pdb
• EMDBエントリー: 62358
• 分子名称: Gene product J, Portal protein (2 entities in total)
• 機能のキーワード: portal, adaptor, phage, viral protein
• 由来する生物種: Escherichia phage Mu (Bacteriophage Mu); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 872339.76

構造登録者

Zhou, J.Q.,Liu, H.R. (登録日: 2024-11-11, 公開日: 2025-02-12, 最終更新日: 2025-07-23)

主引用文献

Zhou, J.,Wang, L.,Xiao, H.,Chen, W.,Liu, Z.,Song, J.,Zheng, J.,Liu, H.
In situ structures of the contractile nanomachine myophage Mu in both its extended and contracted states.
J.Virol., 99:e0205624-e0205624, 2025

PubMed Abstract: Myophage Mu is a representative of contractile nanomachines with a simple tail baseplate. It has the capacity to infect a range of intestinal bacteria and has extensive applications in genetic engineering research. Nevertheless, a comprehensive understanding of the entire structure and contractile mechanisms of Mu remains elusive. Using cryo-electron microscopy (cryo-EM), we resolved the asymmetric structures of Mu in both its extended and contracted states, the latter of which lacked the tail baseplate, at near-atomic resolutions. We built the atomic models for the extended Mu, encompassing the head, the connector complex, the tail, and the simple baseplate. It is noteworthy that we identified the position and structure of the tail tube initiator protein gp43 (referred to as the DNA circularization protein). The protein gp43 plays a crucial role not only in the baseplate assembly and DNA circularization but also in stabilizing the wedge-hub connection and mediating tail contraction. Except for the baseplate structure, the structural comparison of Mu in its extended and contracted states revealed that only the tail sheath protein gp39 and the C-terminus of the tail terminator protein gp37 undergo notable conformational changes to accommodate the tail contraction, whereas the remaining protein components remained unchanged. Our structures exhibited conserved properties among the majority of myophages, thereby providing valuable insights into the contraction mechanisms across myophages and contractile injection systems (CISs).

PubMed: 39992138
DOI: 10.1128/jvi.02056-24

実験手法

ELECTRON MICROSCOPY (3.4 Å)