1. Structural Catalytic Core of the Members of the Superfamily of Acid Proteases
- Author
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Alexander I. Denesyuk, Konstantin Denessiouk, Mark S. Johnson, and Vladimir N. Uversky
- Subjects
pepsin ,retropepsin ,Ddi1 ,Lpg0085 ,acid protease ,three-dimensional structure ,Organic chemistry ,QD241-441 - Abstract
The superfamily of acid proteases has two catalytic aspartates for proteolysis of their peptide substrates. Here, we show a minimal structural scaffold, the structural catalytic core (SCC), which is conserved within each family of acid proteases, but varies between families, and thus can serve as a structural marker of four individual protease families. The SCC is a dimer of several structural blocks, such as the DD-link, D-loop, and G-loop, around two catalytic aspartates in each protease subunit or an individual chain. A dimer made of two (D-loop + DD-link) structural elements makes a DD-zone, and the D-loop + G-loop combination makes a psi-loop. These structural markers are useful for protein comparison, structure identification, protein family separation, and protein engineering.
- Published
- 2024
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