Structure determination and Characterization of proline-specific aminopeptidases

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Proline-specific aminopeptidases are critical to the degradation of proline-rich peptides and proteins, such as collagen and its denatured form, gelatin. Collagens are the largest components in animal tissues and the most major hard-to-degrade proteins because of their unique fibrils composed of triple helical wound polypeptides. In this study, we crystallized three of the recombinant enzymes (Pz-A, Pz-B, and AM-1), and performed its preliminary X-ray crystallographic analysis. We have determined the entire structure of the these aminopeptidases, found a very unique apical domain sharing the interface with a domain containing a main active site and described about the characteristic structure and mechanism for the substrate recognition for proly peptides.