Expression, purification, crystallization and structure of Glyceraldehyde-3-Phosphate Dehydrogenase from Candida albicans, main causative agent of candidiasis

Abstract

Glyceraldehyde-3-phosphate dehydrogenase from Candida albicans (CaGAPDH) is considered a therapeutic target for candidiasis. In this context, we report here the heterologous production, the three dimensional (3D) structure solution and some structural analyses and comparisons of CaGAPDH. The enzyme was expressed, purified and crystallized to collect X-ray diffraction data at the limit of 2.68 Å resolution, presenting some degree of translational non-crystallographic symmetry. Compared with other GAPDH sequences, CaGAPDH presents two paired mutations, Glu296 in place of a common Ala, and Ala258 in place of common Lys/Asn, which stand face to face, therefore, hydrophilic/hydrophobic residues in interchanged positions in CaGAPDH.