Fig. 3
From: BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin
Detailed views of the c-di-GMP-induced domain movement and assembly of two distant c-di-GMP binding sites. a Structural superimpositions of the apo-BrlR (cyan and light cyan) and the c-di-GMP-bound BrlR (magenta and light magenta). b Superimposition of BrlR and c-di-GMP-bound BrlR in a monomer shows that the central helical linker of BrlR is flexible and two terminal domains undergo a clear rigid body movement after c-di-GMPs binding. c A close-up stereoview of the c-di-GMP binding site 1, the residues in contact with C2E1 and around the unique interface of BrlR homotetramer and undergo substantial repositioning after c-di-GMP binding. d A close-up stereoview of c-di-GMP binding site 2, the side chains of the residues in contact with C2E2 and the α-helices to which they belong, which twist significantly after c-di-GMP binding. e The DNA binding domain are shown as surface representations and colored according to their “in vacuum” electrostatics (red for negatively charged regions, and blue for positively charged regions, Pymol). Apo-BrlR is on the upper layer, and c-di-GMP-bound BrlR is on the lower layer. Secondary-structure elements and residues referred to in the text are labeled in Apo-BrlR (red) and the c-di-GMP-bound BrlR (black)
