Fig. 8From: An intrinsically disordered linker controlling the formation and the stability of the bacterial flagellar hookAnalysis of the effect of mutations in the structural context of the hook. Analysis of the different mutations in the ID-Rod-Stretch: (a) Lys32 of S. enterica FlgE, a conserved residue of the ID-Rod-Stretch, is located in a pocket with Asp62, Arg95, and Glu361 in this theoretical model. Both Arg95 and Glu361 are conserved in the FlgE protein family. b Two of the three molecules of FlgE, at position “-5” (cyan) and “-11” (light brown), which interact with the modeled ID-Rod-Stretch of the flagellar hook of S. enterica. Mutations in the ID-Rod-Stretch that are in the interactive domains will affect the stability of the hook. The cryo-electron microscopy structure, including ID-Rod-Stretch of FlgE from C. jejuni [19] (c), is longer than in S. enterica and it is shown here interacting with four FlgE molecules in positions “-5” (cyan), “-10” (green), “-11” (light brown), and “-16” (purple). d Reducing the length of the disordered segment of C. jejuni FlgE reduces its number of interactions with other FlgE molecules in the hook. This has a negative effect on the cohesion of the hookBack to article page