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8YMC

FtsEX in nanodisc

8YMC の概要
エントリーDOI10.2210/pdb8ymc/pdb
EMDBエントリー39394
分子名称Cell division ATP-binding protein FtsE, Cell division protein FtsX, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
機能のキーワードftse, ftsx, gram-negative bacteria, cell division, membrane protein
由来する生物種Escherichia coli K-12
詳細
タンパク質・核酸の鎖数4
化学式量合計127168.34
構造登録者
Chang, S.,Dong, H.,Tang, X. (登録日: 2024-03-08, 公開日: 2025-03-12, 最終更新日: 2026-03-25)
主引用文献Chen, Y.,Guo, D.,Wang, X.,Zhang, C.,Chen, Y.,Luo, Q.,Chen, Y.,Yang, L.,Zhang, Z.,Hong, T.,Zhang, Z.,Dong, H.,Chang, S.,Hu, J.,Tang, X.
Structural insights into the mechanotransducing mechanism of FtsEX in cell division.
MedComm (2020), 5:e688-e688, 2024
Cited by
PubMed Abstract: The filamentous temperature-sensitive (Fts) protein FtsEX plays a pivotal role in () cell division by facilitating the activation of peptidoglycan hydrolysis through the adaptor EnvC. FtsEX belongs to the type VII ATP-binding cassette (ABC) transporter superfamily, which harnesses ATP energy to induce mechanical force, triggering a cascade of conformational changes that activate the pathway. However, the precise mechanism by which FtsEX initiates mechanotransmission remains elusive. Due to the inherent instability of this type of ABC transporter protein in vitro, the conformation of FtsEX has solely been determined in the stabilized ATP-bound state. To elucidate the dynamics of FtsEX, we characterized FtsEX and EnvC of various functional structures through cryo-electron microscopy (cryo-EM) and homology modeling. We validated the structures by molecular dynamics simulations. By site-directed mutagenesis and phenotype screening, we also identified the functional residues involved in allosteric communication between FtsE and FtsX as well as FtsX and EnvC. Additionally, we discovered a potential role of phospholipids in stabilizing the complex conformation during mechanotransmission. This comprehensive exploration significantly enhances our understanding of the intricate mechanisms governing bacterial cell division and unveils potential molecular targets for developing innovative antimicrobial drugs to combat antibiotic resistance.
PubMed: 39434966
DOI: 10.1002/mco2.688
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.7 Å)
構造検証レポート
Validation report summary of 8ymc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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