9UKV

JM Complex - E. coli MurJ, Levivirus M lysis protein LysM (SglM)

9UKV の概要

• エントリーDOI: 10.2210/pdb9ukv/pdb
• EMDBエントリー: 64256
• 分子名称: Lipid II flippase MurJ, Lysis protein (2 entities in total)
• 機能のキーワード: phage, lysis protein, complex, viral protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63636.30

構造登録者

Kohga, H.,Lertpreedakorn, N.,Tsukazaki, T. (登録日: 2025-04-18, 公開日: 2025-09-10, 最終更新日: 2026-03-04)

主引用文献

Kohga, H.,Lertpreedakorn, N.,Miyazaki, R.,Wu, S.,Hosoda, K.,Tanaka, H.,Takahashi, Y.S.,Yoshikaie, K.,Kuruma, Y.,Shigematsu, H.,Mori, T.,Tsukazaki, T.
Phage lysis protein Lys M acts as a wedge to block MurJ conformational changes.
Sci Adv, 11:eady8083-eady8083, 2025

PubMed Abstract: Many antibiotics target essential cellular processes. To combat multidrug-resistant bacteria, new antibacterial strategies are needed. In the peptidoglycan biogenesis pathway in , MurJ, the lipid II flippase, is an essential membrane protein. The 37-residue protein M from the phage, known as Lys or Sgl, targets MurJ and induces cell lysis; however, its molecular mechanism remains unclear. Here, we present the cryo-EM structure of the MurJ/Lys (JM) complex at 3.09-angstrom resolution, revealing that Lys interacts with the crevasse between TM2 and TM7 of MurJ, locking MurJ in an outward-facing conformation, with Lys acting like a wedge. Alanine-scanning mutagenesis and pull-down assays revealed key residues responsible for Lys function, and molecular dynamics simulations showed that Lys stabilizes MurJ's outward-facing state. These findings demonstrate an unprecedented phage-derived mechanism for blocking lipid II transport, providing a structural framework for designing MurJ-targeted antimicrobial agents.

PubMed: 41061077
DOI: 10.1126/sciadv.ady8083

実験手法

ELECTRON MICROSCOPY (3.05 Å)