UC Santa Barbara

The interface between the membrane (MS) and cytoplasmic (C) rings of the bacterial flagellar motor couples torque generation to rotation within the membrane. The structure of the C-terminal helices of the integral membrane protein FliF (FliF_C) bound to the N terminal domain of the switch complex protein FliG (FliG_N) reveals that FliG_N folds around FliF_C to produce a topology that closely resembles both the middle and C-terminal domains of FliG. The interface is consistent with solution-state nuclear magnetic resonance, small-angle X-ray scattering, in vivo interaction studies, and cellular motility assays. Co-folding with FliF_C induces substantial conformational changes in FliG_N and suggests that FliF and FliG have the same stoichiometry within the rotor. Modeling the FliF_C:FliG_N complex into cryo-electron microscopy rotor density updates the architecture of the middle and upper switch complex and shows how domain shuffling of a conserved interaction module anchors the cytoplasmic rotor to the membrane.