Figure 8: Nature Communications

Fig. 8

From: Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc

Fig. 8

Large rotational movement of the PDZ domain and sensing of the bound PDZ ligand by the hinge residues in Prc. a Superimposition of the structures of two Prc molecules (chains C and D colored in green and orange, respectively), D1P (gray), and the resting form of CtpB (yellow), which reveals the hinge residues L340 and L245 and suggests a large rigid-body rotation of the PDZ domain of Prc during its proteolytic action. For clarity only the portions of the proteases connecting to the PDZ domains are shown, in two orthogonal views. The substrate passage perpendicular to the page plane is indicated by the black triangle. The r.m.s.d. between aligned Prc and CtpB (sequence identity: 26%) and between aligned Prc and D1P (sequence identity: 25.4%) are 3.09 Å (for 280 residues) and 2.78 Å (for 202 residues), respectively. b Stereo view of the interaction between the PDZ and NHD domains, colored in gold and blue ribbons, respectively, in Prc (chain C). c Stereo view of the hinge residues L245 and L340 interacting with the peptide ligand bound to the PDZ domain of Prc (chain C)