Fig. 4: Overall structure of CccR.
From: A secreted effector with a dual role as a toxin and as a transcriptional factor
a Cartoon mode of the structure of CccR. Ribbon mode of the overall structure of CccR. The FIC domain contains an α helical structure (residues 1–80, purple), an active center structure (residues 81–275, blue) and an HTH domain (residues 276–380, green). b Interaction analysis of the dimeric interfaces between the two monomers of CccR. The residues involved in the interactions are shown as sticks. c Electrostatic surface potential of CccR. The CccR features of positively charged patches; blue and red indicate positive and negative charges, respectively, and the distance between them in the dimer is indicated. d Molecular docking of CccR with ATP. The conformation with the lowest docking energy was determined using Chimera software. Key residues of CccR involved in ATP binding are shown as purple sticks, and ATP is shown as green sticks. Two potential hydrogen bonds are indicated by dashed lines.
