Open AccessStructure of glycerol‐3‐phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 Å resolution
Author(s) -
Alarcon David Aparicio,
Nandi Munmun,
Carpena Xavi,
Fita Ignacio,
Loewen Peter C.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112037736
Subject(s) - glycerol , dehydrogenase , glycerol 3 phosphate dehydrogenase , biochemistry , dihydroxyacetone phosphate , saccharomyces cerevisiae , dihydroxyacetone , phosphate , chemistry , biology , enzyme , yeast
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.