Extended Data Fig. 6: Comparison of PaFtsWIQBL cryo-EM structure with previous crystal structures of FtsI, FtsQ and RodA.
From: Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL
a) Superposition of FtsI determined by X-ray crystallography (PDB: 3PBN, grey) with the FtsI part of PaFtsWIQBL cryo-EM structure. The TP active site residue S294 is indicated (RMSD of 0.708 Å across 372 pruned atom pairs). b) Superposition of FtsQB determined by X-ray crystallography (PDB: 6H9N in dark grey, PDB: 5Z2W in light grey) with the same area in the cryo-EM structure determined here (For alignment of FtsQ: RMSD (FtsQ-6H9N) of 1.186 Å across 86 pruned atom pairs, RMSD (FtsQ-5Z2W) of 1.118 Å across 95 pruned atom pairs). c) Superposition of RodA determined by X-ray crystallography (PDB: 6BAS in dark grey (left and right), PDB: 6PL5 in light gray (right)) and FtsW in the cryo-EM structure. The position of FtsI is indicated as a transparent blue outline. Apart from transmembrane helix 7, the structures align very well (RMSD (FtsW-6PL5) of 1.188 Å across 202 pruned atom pairs; RMSD (FtsW-6BAS) of 1.126 Å across 206 pruned atom pairs). d) Electrostatic surface representation of PaFtsW viewed from the periplasmic side. A deep cleft is visible that contains the putative active site residue D275. The same representation showing sequence conservation of FtsW mapped onto the surface representation shows that this cleft is highly conserved. Additionally, interaction sites with FtsI and FtsL are indicated; these also show above average levels of sequence conservation.
