Extended Data Fig. 4: Architecture of the PaFtsWIQBL complex.
From: Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL
a) Upper left panel: schematic of the transmembrane helices of FtsW, FtsI, FtsL and FtsB. Two extracellular loops of FtsW that could not be build due to missing density and the N- and C-terminal tails of FtsW are indicated by doted lines. Lower left panel: top view of the transmembrane domain, with FtsW transmembrane helices consecutively numbered based on the sequence (identical to numbering of helices in a previous RodA structure23). FtsW’s putative active site residue D275 is indicated. Right panel: Labelling of the different domains in FtsQ, FtsL, FtsB and FtsI that was used throughout the paper. b) Cryo-EM density showing PaFtsWIQBL within the Lauryl Maltose Neopentyl Glycol (LMNG) detergent micelle, which was subtracted during the later processing stages. c) Prediction of the position and orientation of the divisome core complex transmembrane segments in the lipid bilayer using the Orientations of Proteins in Membranes webserver9. The membrane plane is indicated with two grey discs and the active sites of FtsW and FtsI are labelled. d) A low-resolution structure obtained after fewer 3D classifications shows additional density for FtsQPOTRA at low contour levels and indicates that the transmembrane segment of FtsQ is most likely not part of the micelle that contains the other TM segments. Alignment of a previous FtsB:FtsQ crystal structure (PDB: 6H9N) on FtsQβ shows that FtsQβ and FtsQPOTRA adopt different conformations relative to each other.
