Fig. 7: Structural comparison of ATP-free FtsEX/RipC and ATP-bound FtsEE165QX/RipC complexes.
From: Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis
a PG hydrolysis assay of FtsEX/RipC with non-hydrolysable ATPγS. Differs from PaeFtsEX system, no significant PG hydrolytic activity was observed for MtbFtsEX in the presence of ATPγS. n = 3 replicates, error bars were presented as mean ± SD. Two-tailed unpaired t-test was applied; ***P < 0.0005, n.s. no significant difference. The P-values are shown in figure and source data are provided as a Source Data file. b Cryo-EM density map of the ATP-bound FtsEE165QX/RipC complex. Structures of FtsEX and RipC are represented by purple licorice. The EM density is in gray with 60% transparency, ATP are represented by green surface. c Superposition of the ATP-free FtsEX/RipC (in yellow) and ATP-bound FtsEE165QX/RipC (in purple); Overall, no large conformational changes were observed. For Side view, the FtsEX components are shown as transparent surfaces, and the RipC hydrolase is represented in licorice form. For front view, FtsEX/RipC components are shown as ribbon. d Conformational changes of FtsE upon ATP binding. e Conformational changes in ECD observed during the transition from ATP-free to ATP-bound state. RipC is shown with 70% transparency. f RipC shows no significant movement upon ATP binding prior to ATP hydrolysis.
