TY - JOUR
T1 - The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc- Oxy) and Acid–Base zones
AU - Denessiouk, Konstantin
AU - Denesyuk, Alexander
AU - Permyakov, Sergei E.
AU - Permyakov, Eugene A.
AU - Johnson, Mark
AU - Uversky, Vladimir N.
PY - 2024/1
Y1 - 2024/1
N2 - 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
AB - 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
KW - SGNH-Hydrolases
KW - Catalytic triad
U2 - 10.1016/j.crstbi.2023.100123
DO - 10.1016/j.crstbi.2023.100123
M3 - Article
SN - 2665-928X
VL - 7
JO - Current Research in Structural Biology
JF - Current Research in Structural Biology
M1 - 100123
ER -