Structure of glycerol-3-phosphate dehydrogenase (GPD1) fromSaccharomyces cerevisiaeat 2.45 Å resolution

Abstract

The interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism and providesSaccharomyces cerevisiaewith protection against osmotic and anoxic stress. The first structure of a glycerol-3-phosphate dehydrogenase fromS. cerevisiae, GPD1, is reported at 2.45 Å resolution. The asymmetric unit contains two monomers, each of which is organized with N- and C-terminal domains. The N-terminal domain contains a classic Rossmann fold with the (β-α-β-α-β)2motif typical of many NAD+-dependent enzymes, while the C-terminal domain is mainly α-helical. Structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases and reveal that theClostridium acetobutylicanprotein with PDB code 3ce9 is a glycerol-1-phosphate dehydrogenase.