Fig. 4: Structural comparison of the YejM/LapB and YejM/LPS complexes and protease assays with reconstituted proteoliposomes.
From: Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli
a Structural comparison of the YejM_C molecule (purple, residues 210-YPMTARRF-217 in the linker region colored in orange) and the crystal structure of YejM (green, residues 210-YPMTARRF-217 in the linker region colored in dark yellow) (PDB ID: 6XLP), by superimposing the TM domains with an RMSD of 1.22 Å in the main chains. The orientations of the linker in the two structures are highlighted with dashed lines. b Side and top views of the TM domains of the YejM_C and the LapB dimer. c Side and top views of the TM domain of YejM with an LPS molecule (shown as spheres) in the crystal structure. d Protease activity on LpxC of proteoliposomes reconstituted with FtsH, FtsH/LapB, FtsH/LapB/YejMWT, or FtsH/LapB/YejM3D (with mutations ofT213D/R215D/R216D). The activity of FtsH-proteoliposomes is set to 1, and the activities of all the other proteoliposomes are normalized to it. Each experiment was repeated three times and all data were presented as mean values with error bars representing standard deviations (SDs) of triplicates. Source data for (d) are provided as a Source Data file.
