Probing the mechanism of peptidoglycan amidase activation by FtsEX-EnvC.

This study delves into the mechanism behind the FtsEX-EnvC system, a key component of the E. coli cell division machinery that regulates the breakage of the peptidoglycan layer during daughter cell separation. Through site-directed mutagenesis, the researchers identified mutations that disrupt the autoinhibition mechanism of FtsEX-EnvC, as well as a variant that prevents activation. They also developed a cysteine locking residue pair that stabilizes the complex in its amidase-activating conformation. These findings enhance our understanding of the intricate conformational changes and regulatory mechanisms underlying the precise control of peptidoglycan hydrolysis during bacterial cell division, with implications for potential therapeutic interventions targeting this critical process.