Extended Data Fig. 9: Motor states of Rho hexamer.
From: Structural basis of Rho-dependent transcription termination
(a) Left, superimposition of structure of λtR1-NusG-Rho-TEC (coloured as in Fig. 2a, left) on crystal structure of Rho hexamer interacting with SBS ligand and Mg-ADP-BeF3 in absence of NusG and TEC (PDB 5JJI; coloured grey)22. View orientation as in Fig. 2a, left. TEC omitted for clarity. Right, superimposition of Rho protomers A-F interacting with PBS ligand, SBS ligand, and Mg-ADP-BeF3 in structure of λtR1-NusG-Rho-TEC (coloured as in a) on crystal structure of Rho protomers A-F interacting with SBS ligand and Mg-ADP-BeF3 (PDB 5JJI; grey)22. (b) Occupancy and order of ATP-binding sites of λtR1-NusG-Rho-TEC. Figure presents EM density (blue mesh) and fit (cyan for Rho; orange, light orange, and yellow for Mg-ADP-BeF3 at high, low, and very low occupancies, respectively) for ATP binding sites between Rho protomers A and B, B and C, C and D, D and E, E and F, and F and A.
