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. 2020 Apr 2;11:1641. doi: 10.1038/s41467-020-15490-8

Fig. 4. Putative regulatory role of helix α3.

Fig. 4

a Hydrophobic interactions mediate the association of the C-terminal helix α3 (yellow) with the central β-sheet (gray) in the SepF protomer. b Overall structure of the unliganded SepFΔML homodimer color coded according to temperature factors, from blue (lowest values) to red (highest values). c Deletion of helix α3 in SepFΔML,Δα3 promotes the tight interaction between opposite β-sheets from different SepF dimers, leading to the formation of linear SepF polymers (see also Supplementary Fig. 13).