Article info Vol. 6  No. 3   pp.  71 ~ 74
Title Purification, crystallization, and X-ray crystallographic analysis of histidine triad nucleotide-binding protein from Candida albicans
Authors Ahjin Jung, Shinae Kim and Jeong Ho Chang*
Institutions Department of Biology Education, Kyungpook National University, Daegu 41566, Republic of Korea *Correspondence: jhcbio@knu.ac.kr
Abstract Histidine triad nucleotide-binding protein (HINT) is a member of the histidine triad (HIT) superfamily, and exhibits dinucleotide hydrolase activity via a histidine triad motif. HITs are divided into five classes that have various functions including galactose metabolism, DNA repair, and tumor suppression. Although multiple crystal structures have been reported, limited structural information is available for HINT proteins of fungal species. In this study, to understand the structural features and functional diversity of HINT proteins, we crystallized HINT from four fungal species and obtained X-ray diffraction data from the pathogenic fungus Candida albicans at a resolution of 2.5 Å. The crystal of the C. albicans HINT (CaHINT) belonged to the space group of P2221, with unit cell parameters a = 40.4, b = 101.9, c = 175.2 Å, α = β = γ = 90°. The crystal contained four macromolecules in asymmetric units.