Fig. 4: Electrostatic surface potential and sequence conservation of the rod and LP ring.
From: Structure of the molecular bushing of the bacterial flagellar motor
a Electrostatic potential of the outer surface of the distal rod and the inner surface of the LP ring. The helical arrangement of Asp-109 (circle), Asp-154 (square) and Glu-203 (triangle) of FlgG on the surface of the rod form negatively charged patches. Asp-86, Glu-104 and Asp-78 of FlgH (square) form a negatively charged belt on the inner surface of the L ring. Lys-69 and Lys-114 (triangle) of FlgH and Lys-63 and Lys-95 (circle) of FlgI form positively charged belts on the inner surface of the LP ring. b Conservation of amino acid residues on the outer surface of the distal rod and the inner surface the LP ring. Asp-109 (circle) and Aps-154 (square) of the rod and Lys-63 and Lys-95 (circle) of the P ring are highly conserved. The sequence conservation is colored from cyan to magenta (range of 0–100%), calculated and visualized by Chimera50.
