Fig. 5: A unique inclined binding mode of RipC by MtbFtsEX.
From: Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis
a Comparison of the cryo-EM structure of RipC-bound MtbFtsEX complex and the EnvC-bound PaeFtsX complex (PDB code: 8I6O) (EM density is shown in two orientations). EnvC binds close to the central axis of FtsEX and results in an elongated conformation, while RipC binds at a largely inclined angle with respect to the central axis of FtsEX. b Comparison of ECD/PLD orientation between RipC-bound MtbFtsEX and EnvC-bound PaeFtsX-PLD (PDB code: 8I6O). The surface representations of the ECD/PLD domains are shown, with the upper lobe of the ECD/PLD colored yellow and the lower lobe colored green. RipC and EnvC are represented by ribbon and indicated by red color. UL upper lobe, LL lower lobe. The orientation of the ECD/PLD domain is indicated by arrow. c Comparison between the two ECDFtsX monomers from RipC-bound MtbFtsEX complex. The two ECD monomers along with the connecting hinge region are represented by ribbon. the upper lobe of ECDFtsX is colored in yellow, and the lower lobe of ECDFtsX is in green, the TM1 and TM2 are in blue. Specifically, the hinge region from TM1 is highlighted in red, which exhibits highly dynamic features and determines the orientation of the connecting ECD.
