Fig. 6: Structural comparison of apo and RipC-bound MtbFtsEX.
From: Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis
a Structural rearrangement of the ECD of FtsEX upon RipC binding. The full complex is in front view, the zoom-in views of ECD region is shown in top view and represented by surface. Color scheme: upper lobe in yellow, lower lobe in green; for RipC, α1 in plum, lip in purple, α2 in red, pro-rich linker in blue, the NlpC/P60 catalytic domain in cyan. UL upper lobe, LL lower lobe. b RipC binding triggers ECD1 to rotate in to grasp RipC, while ECD2 shows no significant movement. Structures are represented by ribbon, the Q112 is shown with sticks. RipC is with 70% transparency. c Switch between a straight and a kinked conformation of the hinge region of the TM1, controls the orientation of the linked ECD monomer for RipC binding. Color scheme: Kink region in magenta, short helix in purple, C73-C78 disulfide bridge in cyan. Bound RipC is with 70% transparency.
