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Peer-reviewedCC BY 4.0eLife

Structural insights into peptidoglycan hydrolysis by the FtsEX system in Escherichia coli during cell division

  • Jianwei Li1
  • Yutong He1
  • Xin Xu1
  • Martin Alcorlo2
  • Jian Shi3
  • Souvik Naskar4
  • Nicholas S Briggs4
  • David I Roper4
  • Juan A Hermoso2
  • Lok-To Sham5
  • Min Luo1,3
5 affiliations
  1. 1Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.
  2. 2Department of Crystallography and Structural Biology, Instituto de Química-Física "Blas Cabrera",CSIC, Madrid, Spain.
  3. 3Center for Bioimaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore, Singapore.
  4. 4School of Life Sciences, University of Warwick, Coventry, United Kingdom.
  5. 5Infectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
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Abstract

Bacterial cell division relies on precise peptidoglycan (PG) remodeling, a process orchestrated by the FtsEX complex. Comprised of FtsE and FtsX, this complex collaborates with EnvC, a periplasmic lytic enzyme activator, to regulate septal PG hydrolysis by amidases like AmiB. While recent structural investigations, particularly of Pseudomonas aeruginosa FtsEX (PaeFtsEX), have shed light on complex interactions and proposed activation mechanisms, the structural intricacies governing PG degradation by the FtsEX complex and EnvC in Escherichia coli cytokinesis remain unexplored. In this study, we present a comprehensive biochemical and structural analysis of E. coli FtsEX complexes, unveiling a key role for ATP in complex stabilization that extends across bacterial species. Upon EnvC binding, ATPase activity markedly increases. High-resolution structures of EcoFtsEX, both in the presence and absence of EnvC, reveal a symmetrical conformation of EcoFtsEX capable of accommodating the inherent asymmetry of EnvC, mediated by flexible loops within the periplasmic domain. Our negative-staining imaging showcases an elongated EcoFtsEX/EnvC/AmiB complex reminiscent of the PaeFtsEX system. These findings collectively provide intricate insights into the regulation of PG cleavage by FtsEX in E. coli—a pivotal model system used in pilot genetic studies, suggesting a conserved mechanism for precise hydrolase activation in bacteria.

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Cite

BibTeXRIS
BibTeX
@article{li2026structural,
  title = {{Structural insights into peptidoglycan hydrolysis by the FtsEX system in Escherichia coli during cell division}},
  author = {Jianwei Li and Yutong He and Xin Xu and Martin Alcorlo and Jian Shi and Souvik Naskar and Nicholas S Briggs and David I Roper and Juan A Hermoso and Lok-To Sham and Min Luo},
  journal = {eLife},
  year = {2026},
  month = oct,
  doi = {10.7554/elife.94336},
  url = {https://elifesciences.org/articles/94336},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Structural insights into peptidoglycan hydrolysis by the FtsEX system in Escherichia coli during cell division
AU  - Jianwei Li
AU  - Yutong He
AU  - Xin Xu
AU  - Martin Alcorlo
AU  - Jian Shi
AU  - Souvik Naskar
AU  - Nicholas S Briggs
AU  - David I Roper
AU  - Juan A Hermoso
AU  - Lok-To Sham
AU  - Min Luo
PY  - 2026
DA  - 2026/10/28
JO  - eLife
DO  - 10.7554/elife.94336
UR  - https://elifesciences.org/articles/94336
AB  - Bacterial cell division relies on precise peptidoglycan (PG) remodeling, a process orchestrated by the FtsEX complex. Comprised of FtsE and FtsX, this complex collaborates with EnvC, a periplasmic lytic enzyme activator, to regulate septal PG hydrolysis by amidases like AmiB. While recent structural investigations, particularly of Pseudomonas aeruginosa FtsEX (PaeFtsEX), have shed light on complex interactions and proposed activation mechanisms, the structural intricacies governing PG degradation by the FtsEX complex and EnvC in Escherichia coli cytokinesis remain unexplored. In this study, we present a comprehensive biochemical and structural analysis of E. coli FtsEX complexes, unveiling a key role for ATP in complex stabilization that extends across bacterial species. Upon EnvC binding, ATPase activity markedly increases. High-resolution structures of EcoFtsEX, both in the presence and absence of EnvC, reveal a symmetrical conformation of EcoFtsEX capable of accommodating the inherent asymmetry of EnvC, mediated by flexible loops within the periplasmic domain. Our negative-staining imaging showcases an elongated EcoFtsEX/EnvC/AmiB complex reminiscent of the PaeFtsEX system. These findings collectively provide intricate insights into the regulation of PG cleavage by FtsEX in E. coli—a pivotal model system used in pilot genetic studies, suggesting a conserved mechanism for precise hydrolase activation in bacteria.
SN  - 2050-084X
ER  -