4FGW

Structure of Glycerol-3-Phosphate Dehydrogenase, GPD1, from Sacharomyces Cerevisiae

Summary for 4FGW

• Entry DOI: 10.2210/pdb4fgw/pdb
• Descriptor: Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (2 entities in total)
• Functional Keywords: dehydrogenase, nad+, oxidoreductase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: Q00055
• Total number of polymer chains: 2
• Total formula weight: 85831.38

Authors

Aparicio, D.,Munmun, N.,Carpena, X.,Fita, I.,Loewen, P. (deposition date: 2012-06-05, release date: 2012-11-07, Last modification date: 2023-09-13)

Primary citation

Alarcon, D.A.,Nandi, M.,Carpena, X.,Fita, I.,Loewen, P.C.
Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45A resolution
Acta Crystallogr.,Sect.F, 68:1279-1283, 2012

PubMed 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.

PubMed: 23143232
DOI: 10.1107/S1744309112037736

Experimental method

X-RAY DIFFRACTION (2.45 Å)