- EMDB-62362: Baseplate structure of Escherichia phage Mu -
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基本情報
登録情報
データベース: EMDB / ID: EMD-62362
タイトル
Baseplate structure of Escherichia phage Mu
マップデータ
試料
ウイルス: Escherichia phage Mu (ファージ)
タンパク質・ペプチド: x 10種
リガンド: x 2種
キーワード
phage / sheath / tube / VIRAL PROTEIN
機能・相同性
機能・相同性情報
viral genome circularization / symbiont-mediated evasion of DNA end degradation by host / viral tropism switching / virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / virus tail, tube / virus tail, baseplate / virus tail, fiber / viral tail assembly / adhesion receptor-mediated virion attachment to host cell ...viral genome circularization / symbiont-mediated evasion of DNA end degradation by host / viral tropism switching / virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / virus tail, tube / virus tail, baseplate / virus tail, fiber / viral tail assembly / adhesion receptor-mediated virion attachment to host cell / virion component / host cell cytoplasm / symbiont-mediated suppression of host innate immune response / symbiont entry into host cell / DNA binding / metal ion binding 類似検索 - 分子機能
Bacteriophage Mu, Baseplate protein gp46 / : / Phage protein GP46 / Bacteriophage lambda, Tail fiber protein, repeat-2 / DNA circulation, N-terminal / Phage-associated protein Gp45 / : / : / Phage tail fibre repeat / Bacteriophage Mu Gp45, N-terminal ...Bacteriophage Mu, Baseplate protein gp46 / : / Phage protein GP46 / Bacteriophage lambda, Tail fiber protein, repeat-2 / DNA circulation, N-terminal / Phage-associated protein Gp45 / : / : / Phage tail fibre repeat / Bacteriophage Mu Gp45, N-terminal / DNA circularisation protein N-terminus / Mu phage baseplate assembly protein GpP, fourth domain / Baseplate-like, two-layer sandwich fold / Baseplate protein GpP / : / : / Mu phage baseplate assembly protein GpP-like, N-terminal / Baseplate hub protein gp44-like, second domain / Bacteriophage Mu, GpM, tail tube / Phage tail tube protein / Tail sheath protein / : / Long-tail fiber proximal subunit, C-terminal, trimerization domain / Tape measure protein N-terminal / Tape measure protein / Phage baseplate assembly protein V/Gp45 / Bacteriophage Mu-like, Gp48 / : / Bacteriophage Mu-like, Gp48 / : / Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / Baseplate protein J-like / Baseplate J-like protein / Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain 類似検索 - ドメイン・相同性
DNA circularization protein N / Baseplate hub protein gp44 / Tail sheath protein / Tail tube protein / Tail fiber protein S / Baseplate protein gp48 / Baseplate protein gp47 / Baseplate protein gp46 / Baseplate puncturing device gp45 / Probable tape measure protein 類似検索 - 構成要素
National Natural Science Foundation of China (NSFC)
12034006
中国
National Natural Science Foundation of China (NSFC)
32430020
中国
National Natural Science Foundation of China (NSFC)
32071209
中国
引用
ジャーナル: J Virol / 年: 2025 タイトル: structures of the contractile nanomachine myophage Mu in both its extended and contracted states. 著者: Junquan Zhou / Liwen Wang / Hao Xiao / Wenyuan Chen / Zhonghua Liu / Jingdong Song / Jing Zheng / Hongrong Liu / 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 ...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.
ムービー
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基本情報
マップデータ
試料
キーワード
機能・相同性情報
Escherichia phage Mu (ファージ)
データ登録者
中国, 3件 
引用
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emd_62362.png
http://ftp.pdbj.org/pub/emdb/structures/EMD-62362
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