TY - JOUR
T1 - Crystal structure of α-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701
AU - Watanabe, Risa
AU - Arimura, Yasuhiro
AU - Ishii, Yoshitaka
AU - Kirimura, Kohtaro
N1 - Funding Information:
We would like to thank Emeritus Professor Hitoshi Kurumizaka (Waseda University) for the collection of data at SPring-8 (2017A2558).We also thank the beamline scientists at the BL41XU station of SPring-8 for their assistance with the data collection. This paper is a part of the outcome of research performed under a Waseda University Grant for Special Research Projects (2019R-036 (to K.K.)) from Waseda University, Japan.
Publisher Copyright:
© 2020 Elsevier Inc.
PY - 2020/6/4
Y1 - 2020/6/4
N2 - The α-glucosyl transfer enzyme XgtA is a novel type α-Glucosidase (EC 3.2.1.20) 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.
AB - The α-glucosyl transfer enzyme XgtA is a novel type α-Glucosidase (EC 3.2.1.20) 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.
KW - Crystal structure
KW - Glycoside hydrolase family 13
KW - Xanthomonas campestris
KW - α-Glucosidase
KW - α-glucosides
KW - α-glucosylation
UR - http://www.scopus.com/inward/record.url?scp=85082679829&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85082679829&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2020.03.109
DO - 10.1016/j.bbrc.2020.03.109
M3 - Article
C2 - 32247611
AN - SCOPUS:85082679829
SN - 0006-291X
VL - 526
SP - 580
EP - 585
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -