The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc- Oxy) and Acid–Base zones

Konstantin Denessiouk, Alexander Denesyuk*, Sergei E. Permyakov, Eugene A. Permyakov, Mark Johnson, Vladimir N. Uversky*

*Tämän työn vastaava kirjoittaja

Tutkimustuotos: LehtiartikkeliArtikkeliTieteellinenvertaisarvioitu

1 Sitaatiot (Scopus)
87 Lataukset (Pure)

Abstrakti

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
AlkuperäiskieliEnglanti
Artikkeli100123
Sivumäärä9
JulkaisuCurrent Research in Structural Biology
Vuosikerta7
DOI - pysyväislinkit
TilaJulkaistu - tammik. 2024
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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