Purification, crystallization and preliminary X-ray crystallographic analysis of glycosyltransferase-1 from Bacillus cereus

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 70; no. 9; pp. 1228 - 1231
• Main Authors: Hsieh, Yin-Cheng, Chiu, Hsi-Ho, Huang, Yen-Chieh, Fun, Hoong-Kun, Lu, Chia-Yu, Li, Yaw-Kuen, Chen, Chun-Jung
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.09.2014; Wiley Subscription Services, Inc
• Subjects: Bacillus cereus; Bacillus cereus - enzymology; Crystallization Communications; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; glycosyltransferase; Glycosyltransferases - chemistry; glycosyltransferase; Bacillus cereus
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X14014629

Glycosyltransferases (GTs), which are distributed widely in various organisms, including bacteria, fungi, plants and animals, play a role in synthesizing biological compounds. Glycosyltransferase‐1 from Bacillus cereus (BcGT‐1), which is capable of transferring glucose to small molecules such as kaempferol and quercetin, has been identified as a member of the family 1 glycosyltransferases which utilize uridine diphosphate glucose (UDP‐glucose) as the sugar donor. BcGT‐1 (molecular mass 45.5 kDa) has been overexpressed, purified and crystallized using the hanging‐drop vapour‐diffusion method. According to X‐ray diffraction of BcGT‐1 crystals to 2.10 Å resolution, the crystal belonged to space group P1, with unit‐cell parameters a = 54.56, b = 84.81, c = 100.12 Å, α = 78.36, β = 84.66, γ = 84.84°. Preliminary analysis indicates the presence of four BcGT‐1 molecules in the asymmetric unit with a solvent content of 50.27%.