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Comparative view of domains D0 and D1 of the hook of in (d) and (e), respectively.The molecules that make the hook and the rod are colored in grey with one molecule colored in green and its disordered segment colored in purple.An intrinsically disordered segment plays an important role for overall hook stability and for its structural cohesion during motor rotation.

Comparative view of domains D0 and D1 of the hook of in (d) and (e), respectively.

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To pinpoint which parts of the ID-Rod-Stretch are important for the assembly and function of the hook, we performed targeted mutagenesis of conserved residues in the disordered segment of Flg E from in grey with six highlighted molecules of Flg E.

b Zoom-up, stereo view of the core domain of the hook with the disordered segment, represented with spheres, surrounded by molecules of Flg E which it interacts with.

Our experiments show that this segment is required for polymerization and stability of the hook, demonstrating a surprising role for a disordered region in one of the most finely tuned and closely studied macromolecular machines.

This study reveals a detailed functional characteristic of an intrinsically disordered segment in the hook protein.

During the rotation, the rod is held in place by the LP-ring .

Representative structures, plotted every 10th structure, are sorted and colored by energy for the loop model population (scale ranges from blue (500 Rosetta energy units; REU) to red (850 REU)).For a supra-molecular nano-machine like the bacterial flagellum, which consists of several distinct parts with specific characteristics, stability is important.During the rotation of the bacterial flagellar motor, which is located in the membrane, the flagella rotate at speeds between 2 rpm, depending on the bacterial species.For comparison, the sequence of Flg E from ) from different bacteria show that the segment linking domains D0 and D1 is conserved in both Flg E and Flg G proteins.Both software prediction of disordered protein segments and molecular modeling calculations indicate that this segment is intrinsically disordered and highly flexible (Fig. Compared to the segment connecting domains D0 and D1 of the bacterial filament protein Fli C (Leu31-Asp43), the segment in Flg E does not show any clearly defined native state.This linker becomes partly structured upon formation of the hook, where it is located in a pocket surrounded by molecules of Flg E (Fig.), and thus likely shows similar structural behavior.Finding a way of disrupting this linker in Schematic representation of the flagellum from a gram-negative bacterium.The distal rod (green), located in the outer membrane, is in direct contact with the hook (blue).This segment evolved to fulfill a specific role in the formation of the hook, and it is at the core of the stability and flexibility of the hook.Its length is important in the case of bacteria with high-speed rotating flagella.

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