Fig. 6: Interactions between the rod and LP ring and their assembly process.
From: Structure of the molecular bushing of the bacterial flagellar motor
a Vertical section of the atomic model of the rod (gray), L ring (purple), P ring (cyan) with the map of the MS ring at the bottom (gray). Charged amino acid residues are displayed with negative in red (Asp-109, Asp-154, Glu-203 of FlgG and Asp-78, Asp-86, Glu-104 of FlgH) and positive in blue (Lys-69, Lys-114 of FlgH and Lys-63, Lys-95 of FlgI). Four polar residues from Thr-33 to Thr-36 of FlgI in the P ring loop, which is located most closely to the rod surface, are shown in pink. The dashed lines are where the proximal rod is expected to exist. Axial view of four horizontal slices of the rod and LP ring as indicated in a, showing repulsive and attractive interactions between the rod and LP ring: b repulsive interactions; c attractive interactions; d the smallest gap between the rod and LP ring with non-charged residues of FlgI in the P ring loop; e attractive interactions. f The assembly process of the rod (gray) and LP ring (purple and cyan).
