pISSN 2288-6982
eISSN 2288-7105




BioDesign 2022; 10(1): 8-11

Published online March 30, 2022

© Korean Society for Structural Biology

Purification, crystallization and X-ray crystallographic analysis of galactose-1-phosphate uridylyltransferase from Debaryomyces hansenii

Sang Woon Lee1, Hong Ha Vu2 and Jeong Ho Chang1,2,3,*

1Department of Biomedical Convergence Science and Technology, Kyungpook National University, Daegu 41566, Republic of Korea
2Department of Biology Education, Kyungpook National University, Daegu 41566, Republic of Korea
3Research Institute for Phylogenomics and Evolution, Kyungpook National University, Daegu 41566, Republic of Korea

Correspondence to: *

Received: February 4, 2022; Revised: March 9, 2022; Accepted: March 16, 2022


Galactose-1-phosphate uridylyltransferase (GALT) is the second enzyme in the Leloir pathway that reversibly converts galactose-1-phosphate to glucose-1-phosphate. GALT deficiency can cause growth defects in both prokaryotes and eukaryotes. Likewise, in humans, damage of this enzyme leads to a toxic syndrome known as galactosemia type I. In this study, to understand structural features and the underlying molecular mechanism of GALT in yeast, the crystal of GALT from Debaryomyces hansenii was determined at a resolution of 2.8 Å. The crystal of D. hansenii (DhGALT) belonged to the space group C2221, with the unit cell parameters a = 88.5 Å, b = 122.3 Å, c = 154.2 Å, α = β = γ = 90°. Two macromolecules were present in the asymmetric unit of the crystal. Following its structural determination, further study will be done for elucidating the structural features and reaction mechanism in fungal species.