EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	structures of the contractile nanomachine myophage Mu in both its extended and contracted states.
ジャーナル・号・ページ	J Virol, Vol. 99, Issue 3, Page e0205624, Year 2025
掲載日	2025年3月18日
著者	Junquan Zhou / Liwen Wang / Hao Xiao / Wenyuan Chen / Zhonghua Liu / Jingdong Song / Jing Zheng / Hongrong Liu /
PubMed 要旨	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 ...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). IMPORTANCE: Despite extensive study, the asymmetric structures of phage Mu, a highly effective transposable myophage, remain unknown. In this study, we present the high-resolution structures of Mu in both its extended and contracted states. The comparison of the two structures allows for the illustration of detailed conformational changes of the head-to-tail complex during the process of tail contraction. The contraction mechanism of Mu is highly conserved and widely adapted to all contractile nanomachines that share common structural features with Mu.
リンク	J Virol / PubMed:39992138 / PubMed Central
手法	EM (単粒子)
解像度	3.2 - 3.8 Å
構造データ	61659 9jod EMDB-61659, PDB-9jod: Capsid structure of Escherichia phage Mu 手法: EM (単粒子) / 解像度: 3.2 Å 62358 9khx EMDB-62358, PDB-9khx: Neck structure of Escherichia phage Mu 手法: EM (単粒子) / 解像度: 3.4 Å 62359 9khy EMDB-62359, PDB-9khy: Terminator and trunk structure of Escherichia phage Mu 手法: EM (単粒子) / 解像度: 3.4 Å 62362 9ki1 EMDB-62362, PDB-9ki1: Baseplate structure of Escherichia phage Mu 手法: EM (単粒子) / 解像度: 3.3 Å 62462 9knu EMDB-62462, PDB-9knu: Neck structure of bacteriophage Mu in contracted state 手法: EM (単粒子) / 解像度: 3.6 Å 63137 9lj8 EMDB-63137, PDB-9lj8: Tail structure of bacteriophage Mu in contracted state 手法: EM (単粒子) / 解像度: 3.8 Å
化合物	ChemComp-CA: Unknown entry / カルシウムジカチオン ChemComp-FE: Unknown entry
由来	escherichia phage mu (ファージ)
キーワード	VIRAL PROTEIN / capsid / phage / portal / adaptor / sheath / tube / terminator