9J6M

beta-D-galactofuranosidase ORF1110 from Streptomyces sp. JHA19, ligand-free form

Summary for 9J6M

• Entry DOI: 10.2210/pdb9j6m/pdb
• Descriptor: Beta-D-galactofuranosidase 2, GLYCEROL, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: glycoside hydrolase family 2, hydrolase
• Biological source: Streptomyces sp. JHA19
• Total number of polymer chains: 2
• Total formula weight: 135268.73

Authors

Fujio, N.,Yamada, C.,Takegawa, K.,Fushinobu, S. (deposition date: 2024-08-16, release date: 2024-11-27, Last modification date: 2024-12-25)

Primary citation

Fujio, N.,Yamada, C.,Kashima, T.,Matsunaga, E.,Nash, R.J.,Takegawa, K.,Fushinobu, S.
Crystal structure of beta-d-galactofuranosidase from Streptomyces sp. JHA19 in complex with an inhibitor provides insights into substrate specificity.
Febs Lett., 598:2866-2875, 2024

PubMed Abstract: 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 = 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.

PubMed: 39543437
DOI: 10.1002/1873-3468.15056

Experimental method

X-RAY DIFFRACTION (1.8 Å)