Active site mutations in the bacterial actin homolog FtsA impair direct interactions with the divisome in Escherichia coli
J. J. Morrison, C. N. Ferreira, E. M. Siler, K. Nelson, C. E. Trebino, B. Piraino, J. L. Camberg
This study identifies key residues in FtsA critical for ATP hydrolysis, phospholipid binding, and membrane interactions, showing their role in Z-ring assembly and cell division in E. coli.
bioRxiv · Feb 25, 2022 · PreprintMicrobiology