The study delves into the intricate mechanisms of peptidoglycan hydrolysis during cell division in Escherichia coli. It reveals how ATP stabilizes the FtsEX complex, enhances EnvC binding, and activates amidases like AmiB for precise hydrolase activation. The findings shed light on conserved mechanisms across bacterial species and provide valuable insights into bacterial cell division regulation.
The research uncovers a symmetrical conformation of EcoFtsEX capable of accommodating asymmetrical EnvC interactions, elucidating key loops' adaptability for binding. The study also proposes a model for temporal regulation of PG cleavage involving ATP-driven stabilization, EnvC recruitment, and amidase activation by FtsEX.
Overall, the study provides comprehensive insights into the regulatory role of the FtsEX system in bacterial cell division, emphasizing the importance of ATP-dependent stabilization and precise hydrolase activation mechanisms.
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by Li,J., He,Y.... at www.biorxiv.org 01-20-2024
https://www.biorxiv.org/content/10.1101/2024.01.16.575974v1Deeper Inquiries