Article
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Structural Catalytic Core of the Members of the Superfamily of Acid Proteases
Version 1
: Received: 21 June 2024 / Approved: 22 June 2024 / Online: 24 June 2024 (11:25:52 CEST)
A peer-reviewed article of this Preprint also exists.
Denesyuk, A.I.; Denessiouk, K.; Johnson, M.S.; Uversky, V.N. Structural Catalytic Core of the Members of the Superfamily of Acid Proteases. Molecules 2024, 29, 3451. Denesyuk, A.I.; Denessiouk, K.; Johnson, M.S.; Uversky, V.N. Structural Catalytic Core of the Members of the Superfamily of Acid Proteases. Molecules 2024, 29, 3451.
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 packs all conserved substructure elements around the catalytic machinery, and which can be found in all enzymes of the Acid proteases superfamily. The SCC is a dimer of several structural blocks, such as the DD-link, the D-loop and the G-loop, around two catalytic aspartates in each protease subunit or within an individual chain. The dimer of two D-loop/DD-link substructures makes a DD-zone, and the dimer of two D-loop/G-loop substructures makes a psi-loop. These structural markers are useful for protein comparison, structure identification, protein family separation and protein engineering.
Keywords
Pepsin; Retropepsin; Ddi1; Lpg0085; Acid protease; three-dimensional structure; active site; catalytic aspartate
Subject
Biology and Life Sciences, Life Sciences
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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