| Title : The active site of the SGNH hydrolase-like fold proteins: Nucleophile-oxyanion (Nuc-Oxy) and Acid-Base zones - Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| Author(s) : Denessiouk K , Denesyuk AI , Permyakov SE , Permyakov EA , Johnson MS , Uversky VN |
| Ref : Curr Res Struct Biol , 7 :100123 , 2024 |
| 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. |
| ESTHER : Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| PubMedSearch : Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| PubMedID: 38235349 |
Denessiouk K, Denesyuk AI, Permyakov SE, Permyakov EA, Johnson MS, Uversky VN (2024)
The active site of the SGNH hydrolase-like fold proteins: Nucleophile-oxyanion (Nuc-Oxy) and Acid-Base zones
Curr Res Struct Biol
7 :100123
Denessiouk K, Denesyuk AI, Permyakov SE, Permyakov EA, Johnson MS, Uversky VN (2024)
Curr Res Struct Biol
7 :100123