Fig. 4: Rof conformational changes upon ρ binding.
a Structure of ecRof in isolation. Representative structure (left) and structural ensemble (right) of ecRof determined by NMR spectroscopy (PDB ID: 1SG5)21. The N-termini (N) and helix α1 are colored in orange. C, C-termini. The N-termini of isolated ecRof show high flexibility and are oriented away from the protein’s core. b AlphaFold model of ecRof. Rof is colored according to the AlphaFold model confidence score (pLDDT). The pLDDT score indicates structural flexibility in the N-terminal region, including helix α1. c Isolated ecRof (gray) superimposed on ρ-bound ecRof (violet) in the same view as isolated ecRof in (a). Rotation symbols, view relative to Fig. 2b. In the conformation of isolated ecRof, the N-terminus and helix α1 would sterically interfere with binding to ρ.
