ArticleCurrent research in structural biology2024
The active site of the SGNH hydrolase-like fold proteins: Nucleophile-oxyanion (Nuc-Oxy) and Acid-Base zones.
Article in Current research in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Cloning, Expression, and Characterization of GDSL-Type Lipolytic Enzyme Genes fromJournal of microbiology and biotechnology · 2025Article
- Biodegradation of Poly(ε-caprolactone): Microorganisms, Enzymes, and Mechanisms.International journal of molecular sciences · 2025Review
- Alpha and Omega Classification of β-Lactamase/Transpeptidase-like Superfamily Proteins Based on the Comparison of Their Structural Catalytic Cores.Molecules (Basel, Switzerland) · 2025Article
- Structural Catalytic Core of the Members of the Superfamily of Acid Proteases.Molecules (Basel, Switzerland) · 2024Review
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Authors and funding
6 authors.
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Abstract
SGNH hydrolase-like fold proteins are serine proteases with the default Asp-His-Ser catalytic triad. Here, we show that these proteins share two unique conserved structural organizations around the active site: (1) the Nuc-Oxy Zone around the catalytic nucleophile and the oxyanion hole, and (2) the Acid-Base Zone around the catalytic acid and base. The Nuc-Oxy Zone consists of 14 amino acids cross-linked with eight conserved intra- and inter-block hydrogen bonds. The Acid-Base Zone is constructed from a single fragment of the polypeptide chain, which incorporates both the catalytic acid and base, and whose N- and C-terminal residues are linked together by a conserved hydrogen bond. The Nuc-Oxy and Acid-Base Zones are connected by an SHLink, a two-bond conserved interaction from amino acids, adjacent to the catalytic nucleophile and base.
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