Inviter: 王玉梅（wangym@iphy.ac.cn）

Abstract:
Bacteria must cut their cell wall to divide, yet uncontrolled cleavage can destroy the cell. How do they activate this process at the right place and time? In this talk, I will present structural and functional studies showing how the ATP-powered membrane complex FtsEX controls peptidoglycan cleavage. In Escherichia coli, FtsEX recruits the activator EnvC and uses ATP-dependent conformational changes to promote recruitment and activation of the amidase AmiB. In mycobacteria, FtsEX engages the hydrolase RipC directly, with a distinct binding geometry that suggests how the same regulatory machinery can position cell-wall cleavage differently. I will also discuss emerging structural insights into the FtsEX–FtsZ assembly, connecting hydrolase regulation to the division-site scaffold. Together, these findings explain how an ABC-family machine transmits signals across the membrane to control cell-wall remodelling and reveal adaptations associated with different bacterial division strategies. Understanding this essential process provides a foundation for exploring antibacterial approaches that disrupt the precise control of cell-wall cleavage.

About the speaker:
Dr. Min Luo, Assistant Professor in the Department of Biological Sciences at the National University of Singapore. Dr. Luo received his Ph.D. from the University of Missouri–Columbia and completed his postdoctoral training at Harvard Medical School before joining NUS in 2020. His research uses cryo-electron microscopy to understand the structure and molecular mechanisms of membrane proteins and large macromolecular complexes. His current work focuses on ATP-binding cassette (ABC) transporters involved in bacterial cell division and antibiotic resistance, with particular interest in how higher-order assembly regulates transporter function.