4FGW
Structure of Glycerol-3-Phosphate Dehydrogenase, GPD1, from Sacharomyces Cerevisiae
4FGW の概要
| エントリーDOI | 10.2210/pdb4fgw/pdb |
| 分子名称 | Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (2 entities in total) |
| 機能のキーワード | dehydrogenase, nad+, oxidoreductase |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) |
| 細胞内の位置 | Cytoplasm: Q00055 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 85831.38 |
| 構造登録者 | Aparicio, D.,Munmun, N.,Carpena, X.,Fita, I.,Loewen, P. (登録日: 2012-06-05, 公開日: 2012-11-07, 最終更新日: 2023-09-13) |
| 主引用文献 | 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 Cited by 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: 23143232DOI: 10.1107/S1744309112037736 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






