Figure 10

The differences between the active site residues of parvulins. Comparison of PrsA-PPIase and hPin1 active site residues shows that the highly conserved histidine side-chains have distinct conformations. (A) The active site residues of S. aureus PrsA-PPIase. (B) The hPin1 residues [PDB:1PIN] proposed to participate in the catalysis mechanism. (C) Schematic presentation of the potential charge relay system of S. aureus PrsA-PPIase. Deprotonation of the active site aspartates can be promoted by delocalisation of the negative charge through the active site histidines. Protein structure visualisations were done using PyMol [34].