Fig. 8: Rof conformational changes and conservation. | Nature Communications

Fig. 8: Rof conformational changes and conservation.

From: Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation

Fig. 8

a, b The structure of one E. coli (ec) Rof protein as observed in the ρ-Rof complexes (a) compared to one monomer from the crystal structure of a V. cholerae (vc) Rof dimer (b; PDB ID: 6JIE). EcRof bound to ρ and vcRof mainly differ in the orientation of the N-termini and the lengths of helices α1. N, N-termini; C, C-termini. c Conservation of Rof sequences in Enterobacteriaceae (top) and Vibrionaceae (bottom). In Enterobacteriacea, two alternative start sites for Rof are possible, generating 84- and 86-residue Rof. The interface residues revealed by the E. coli ρ-Rof complex structures are indicated by black dots. Sequence logos were generated by WebLogo (version 3.7.8). d Superposition of the vcRof on ecRof bound to ρ. Upper panel, superposition of a vcRof monomer on ecRof bound to ρ. Lower panel, superposition of the vcRof dimer on ecRof bound to ρ; for clarity, ecRof is not shown. Rotation symbols, view relative to Fig. 2b. While monomeric vcRof would align without steric conflict, there might be steric hindrance in the interaction between a dimer of vcRof and ρ. e The rof and yaeP genes are coupled in Enterobacteriaceae, but not in Vibrionaceae; see Supplementary Data 1 for more details.

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