Figure 2

The reaction catalyzed by CypA (a) CypA is a member of a family of enzymes known as PPIase, which catalyze the cis/trans isomerization of peptide bonds N-terminal to proline residues in peptides and proteins (b) The active-site of CypA with a peptide substrate. The shown substrate has the sequence succinyl(Sin)-Ala-Ala-Pro-Phe-p-nitroanilide(Nit) and is labeled as chain B. The red arrow indicates the catalyzed isomerization. Several residues are conserved for their role in enzyme reaction. The dynamical motion of these hydrophobic and hydrophilic residues is linked to the substrate turnover step [10–12]. The green lines indicate hydrogen bonds between substrate and enzyme, while the hydrophobic interactions are depicted by small red radiating lines.