Fig. 9: FtsEX/RipC complex involved peptidoglycan hydrolysis in Mycobacterium tuberculosis.

a Model showing uneven distribution and/or activation of PG hydrolases that generate a breaking point for V-snapping in Mycobacterium tuberculosis. b Working model for FtsEX regulated RipC activation in Mycobacterium tuberculosis. This model illustrates the transition of the FtsEX/RipC complex from its autoinhibited state (left) to its activated state (right) during peptidoglycan hydrolysis at the division site. Initially, the complex is in its autoinhibited state and unable to cleave the peptidoglycan layer. However, ATP binding and hydrolysis at the cytosolic side initiates a series of conformational changes that ultimately lead to the activation of the complex for peptidoglycan hydrolysis at the division site. Once the hydrolysis is complete, ATP hydrolysis recycles the complex back to its autoinhibited state. Color scheme: FtsX is indicated in cornflower blue/rosy brown, FtsE is indicated in magenta/dark green. For RipC, α1 in plum, lip in purple, α2 in red, pro-rich linker in blue, the NlpC/P60 catalytic domain in cyan.