Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 Å resolution

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1279-83. doi: 10.1107/S1744309112037736. Epub 2012 Oct 26.

Abstract

The interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism and provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The first structure of a glycerol-3-phosphate dehydrogenase from S. 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)2 motif 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 the Clostridium acetobutylican protein with PDB code 3ce9 is a glycerol-1-phosphate dehydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Crystallography, X-Ray
  • Glycerol-3-Phosphate Dehydrogenase (NAD+) / chemistry*
  • Glycerol-3-Phosphate Dehydrogenase (NAD+) / genetics
  • Models, Molecular
  • Molecular Sequence Annotation
  • Phylogeny
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Structural Homology, Protein

Substances

  • Saccharomyces cerevisiae Proteins
  • GPD1 protein, S cerevisiae
  • Glycerol-3-Phosphate Dehydrogenase (NAD+)

Associated data

  • PDB/4FGW