Fig. 2: MdtF has a fixed ‘swung-out’ R2 transmembrane conformation across access and binding states.
From: Molecular basis for multidrug efflux by an anaerobic-associated RND transporter
A Each chain was assigned to the access, binding, or extrusion protomer state within AcrB (PDB: 4DX5)38 according to global RMSD measurements (Cα-atoms). B Localised backbone RMSD calculations (Cα-atoms) reveal regional differences between AcrB and MdtF. C Alignment of AcrB (pink) and MdtF (blue) transmembrane domains, which reveal the structural differences between its helical arrangement as it cycles through the protomeric states. RMSD root mean square deviation, TM transmembrane helix.
