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FtsEX belongs to the type VII ATP\u2010binding 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\u2010bound state. To elucidate the dynamics of FtsEX, we characterized FtsEX and EnvC of various functional structures through cryo\u2010electron microscopy (cryo\u2010EM) and homology modeling. We validated the structures by molecular dynamics simulations. By site\u2010directed mutagenesis and phenotype screening, we also identified the functional residues involved in allosteric communication between FtsE and FtsX as well as FtsX and EnvC. 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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.<\/jats:p>","DOI":"10.1002\/mco2.688","type":"journal-article","created":{"date-parts":[[2024,10,21]],"date-time":"2024-10-21T06:07:18Z","timestamp":1729490838000},"source":"Crossref","is-referenced-by-count":5,"title":["Structural insights into the mechanotransducing mechanism of FtsEX in cell division"],"prefix":"10.1002","volume":"5","author":[{"given":"Yuejia","family":"Chen","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine, State Key Laboratory of Biotherapy, National Clinical Research Center for Geriatrics, West China Hospital Sichuan University  Chengdu China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Du","family":"Guo","sequence":"additional","affiliation":[{"name":"Department of 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