Crystal structure of α-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701

Risa Watanabe, Yasuhiro Arimura, Yoshitaka Ishii, Kohtaro Kirimura*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


The α-glucosyl transfer enzyme XgtA is a novel type α-Glucosidase (EC produced by Xanthomonas campestris WU-9701. One of the unique properties of XgtA is that it shows extremely high α-glucosylation activity toward alcoholic and phenolic –OH groups in compounds using maltose as an α-glucosyl donor and allows for the synthesis of various useful α-glucosides with high yields. XgtA shows no hydrolytic activity toward sucrose and no α-glucosylation activity toward saccharides to produce oligosaccharides. In this report, the crystal structure of XgtA was solved at 1.72 Å resolution. The crystal belonged to space group P22121, with unit-cell parameters a = 73.07, b = 83.48, and c = 180.79 Å. The β→α loop 4 of XgtA, which is proximal to the catalytic center, formed a unique structure that is not observed in XgtA homologs. Furthermore, XgtA was found to contain unique amino acid residues around its catalytic center. The unique structure of XgtA provides an insight into the mechanism for the regulation of substrate specificity in this enzyme.

Original languageEnglish
Pages (from-to)580-585
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 2020 Jun 4


  • Crystal structure
  • Glycoside hydrolase family 13
  • Xanthomonas campestris
  • α-Glucosidase
  • α-glucosides
  • α-glucosylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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