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

Autor: Fujio N; Department of Biotechnology, The University of Tokyo, Japan., Yamada C; School of Agriculture, Meiji University, Kawasaki, Japan., Kashima T; Department of Biotechnology, The University of Tokyo, Japan.; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Japan., Matsunaga E; Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan., Nash RJ; Institute of Biological, Environmental and Rural Sciences/Phytoquest Limited, Aberystwyth, UK., Takegawa K; Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan., Fushinobu S; Department of Biotechnology, The University of Tokyo, Japan.; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Japan.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2024 Nov 14. Date of Electronic Publication: 2024 Nov 14.
DOI: 10.1002/1873-3468.15056
Abstrakt: 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 (K i  = 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.
(© 2024 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Databáze: MEDLINE
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