Crystal structure of β-d-galactofuranosidase from Streptomyces sp. JHA19 in complex with an inhibitor provides insights into substrate specificity

Noriki Fujio, Chihaya Yamada, Toma Kashima, Emiko Matsunaga, Robert J. Nash, Kaoru Takegawa*, Shinya Fushinobu*

*Awdur cyfatebol y gwaith hwn

Allbwn ymchwil: Cyfraniad at gyfnodolynErthygladolygiad gan gymheiriaid

5 Wedi eu Llwytho i Lawr (Pure)

Crynodeb

d-Galactofuranose (Galf) is widely distributed in glycoconjugates of pathogenic microbes. β-d-Galactofuranosidase (Galf-ase) from Streptomyces sp. JHA19 (ORF1110) belongs to glycoside hydrolase (GH) family 2 and is the first identified Galf-specific degradation enzyme. Here, the crystal structure of ORF1110 in complex with a mechanism-based potent inhibitor, d-iminogalactitol (Ki = 65 μm) was solved. ORF1110 binds to the C5–C6 hydroxy groups of d-iminogalactitol with an extensive and integral hydrogen bond network, a key interaction that discriminates the substrates. The active site structure of ORF1110 is largely different from those of β-glucuronidases and β-galactosidases in the same GH2 family. A C-terminal domain of ORF1110 is predicted to be a carbohydrate-binding module family 42 that may bind Galf. The structural insights into Galf-ase will contribute to the investigation of therapeutic tools against pathogens.

Iaith wreiddiolSaesneg
CyfnodolynFEBS Letters
Dyddiad ar-lein cynnar14 Tach 2024
Dynodwyr Gwrthrych Digidol (DOIs)
StatwsE-gyhoeddi cyn argraffu - 14 Tach 2024

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