Fig. 3: The structure of RipC.

a Domain arrangements and overall structure of RipC in an autoinhibited state. The α1 domain is colored in plum, lip in purple, α2 in red, pro-rich linker in blue, the NlpC/P60 catalytic domain in cyan, and the catalytic residues are in orange. b The NlpC/P60 domain is restrained by the N-terminal region of α1. The NlpC/P60 domain is shown in cyan surface, while the residues involved in the interaction with α1 are depicted in plum sticks. c Y288 and W290 of the NlpC/P60 domain (in cyan) are positioned like a wedge, inserted into a shallow groove between α1 and α2 helices. d Interaction between the NlpC/P60 domain and α1 helix blocks access to the catalytic site of NlpC/P60. Catalytic residues are shown in orange sticks. e The initial segment of the Pro-rich linker connecting the CCD with the catalytic domain is stabilized in a long groove of the catalytic domain. Catalytic domain is represented in surface, the CCD is shown in ribbon with 60% transparency.