Fig. 5: Conformational changes within DmpRΔD.
From: Tetrameric architecture of an active phenol-bound form of the AAA+ transcriptional regulator DmpR
a Superimposition of the sensory domains of the P1 protomer (light blue) and the P2 protomer (wheat) to highlight the asymmetry. The region showing significant structural changes is indicated by a dotted box. The movement of several residues in the region connecting helix α6 and the B-linker (blue sticks in the P1 protomer and white sticks in the P2 protomer). The changes in each residue are indicated by the dotted arrows. b Structural flexibility of helix α6 in the sensory domains of MopR (PDB ID, 5kbi, light pink), PoxR (PDB ID, 5fru, yellow) and DmpR (light blue) is represented within a dotted circle. c Superimposition of the DmpR protomer (light blue) onto that of NtrC1 (PDB ID, 1ny5, green) with respect to the ATPase domains to highlight the flexible region and the different trajectories of the B-linker and ATPase domain. d Model of the conformational change of the transition from the inactive DmpR dimer to the tetrameric complex upon the binding of phenol.
