Fig. 1: Biochemical and structural study of MtbFtsEX complex in peptidisc.
From: Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis
a ATPase activity of FtsEX and FtsEX mutants. There are no ATPase activity of mutants FtsED164AX and FtsEE165QX. n = 3 replicates, error bars were presented as mean ± SD. Two-tailed unpaired t-test; **P < 0.005. The P-value is shown in figure. b Pull-down study of RipC binding to FtsEX or its ATPase mutant, in the presence or absence of different nucleotides or analogues. RipC forms a stable complex with FtsEX was ATP independent. Each experiment was repeated three times independently with similar results. c ATPase activity of FtsEX in the presence of RipC. The addition of RipC has no effect on the ATPase activity of FtsEX. n = 3 replicates, error bars were presented as mean ± SD.Two-tailed unpaired t-test; **P < 0.005, n.s. no significant difference. The P-values are shown in figure. d ATPase activity of FtsEX and FtsEX/RipC complex in peptidisc. n = 3 replicates, error bars were presented as mean ± SD. The source data of a–d are provided as a Source Data file. e Domain arrangements and topology diagram of FtsX and FtsE. For FtsX, α helices are shown as cylinder, β sheets are shown as arrows. f Protomer structure of FtsEX in 2 orientations. Color scheme: FtsE in magenta, TMFtsX 1-4, CHFtsX and EHFtsX in cornflower blue, the upper lobe of ECDFtsX in yellow, and the lower lobe of ECDFtsX in light green. CH coupling helix, EH elbow helix, UL upper lobe, LL lower lobe. g Front-view of the cryo-EM density map of FtsEX in the absence of ATP (left), and the ribbon representation of WT FtsEX (right). Color scheme: FtsX in blue and brown, The upper lobe of ECDFtsX in yellow, and the lower lobe of ECDFtsX in light green; FtsE in magenta and dark green. h Top-down view of TMDs with small loop (SL) shown.
