Extended Data Fig. 6: Electron density map for MMF2 bound to MmfR, comparison of the overall fold of the MmfR and CprB monomers and X-ray crystal structures of TFTR–operator complexes.
From: Molecular basis for control of antibiotic production by a bacterial hormone
a, SIGMAA-weighted mFo − ΔFc electron density omit map for MMF2 bound to MmfR in mesh representation contoured at the 5σ level. b, Overall fold of the MmfR monomer. c, Overall fold of the CprB monomer (PDB ID: 4PXI). Both structures are colour-ramped from blue to red from the N to the C terminus. d, X-ray crystal structures of TFTRs that bind as pairs of homodimers in complex with their operators. PDB IDs are as follows: 6EN8 (SaFadR), 6C31 (Rv0078), 4JL3 (Ms6564), 5GPC (FadR), 1JT0 (QacR), 4I6Z (TM1030), 2YVH (CgmR), 4PXI (CprB), 5VL9 (EilR) and 4GCT (SlmA). e, X-ray crystal structures of TFTRs that bind as single homodimers in complex with their operators. PDB IDs are as follows: 1QPI (TetR), 5DY0 (AmtR), 3LSP (DesT), 5UA1 (KstR), 3ZQL (SimR), 5K7Z (AibR), 3VOK (HrtR) and 5YEJ (BioQ). f, Side view of the QacR–operator and CprB–operator complexes highlighting the obtuse angle between the planes that bisect the monomers in each homodimer.
