Abstract

Article info Vol. 7  No. 2   pp.  42 ~ 46
Title Purification, crystallization and X-ray crystallographic analysis of methylglyoxal reductase Gre2 from Candida albicans
Authors Giang Thu Nguyen1, Shinae Kim1, Hang-Suk Chun2, Woo-Keun Kim2,* and Jeong Ho Chang1,*
Institutions 1Department of Biology Education, Kyungpook National University, Daegu 41566, Republic of Korea 2Biosystem Research Group, Korea Institute of Toxicology, Daejeon 34114, Republic of Korea *Correspondence: jhcbio@knu.ac.kr, wookkim@kitox.re.kr
Abstract Methylglyoxal reductase Gre2 converts methylglyoxal to lactaldehyde, using either NADH or NADPH as electron donor, to protect cells from the cytotoxic effects of methylglyoxal. Gre2 belongs to the short-chain dehydrogenase/reductase superfamily, which exhibits considerable variation in its substrate binding clefts to catalyze a broad range of substrates. In this study, to understand the structural features and molecular mechanism of Gre2, we overexpressed, purified, and crystallized the N-terminal His6-tagged Gre2 protein from Candida albicans and obtained X-ray diffraction data at a resolution of 2.8 Å. The C. albicans Gre2 crystal belongs to space group I23 with unit cell parameters a = b = c = 149.6 Å, α = β = γ = 90º. There is one molecule in the asymmetric unit.