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- Title
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
- Authors
Li, M; Phylip, L H; Lees, W E; Winther, J R; Dunn, B M; Wlodawer, A; Kay, J; Gustchina, A
- Abstract
Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
- Publication
Nature structural biology, 2000, Vol 7, Issue 2, p113
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/72378