4UEJ

Closed state of galactitol-1-phosphate 5-dehydrogenase from E. coli in complex with glycerol.

4UEJ の概要

• エントリーDOI: 10.2210/pdb4uej/pdb
• 関連するPDBエントリー: 4UEK 4UEO
• 分子名称: GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75371.36

構造登録者

Benavente, R.,Esteban-Torres, M.,Kohring, G.W.,Cortes-Cabrera, A.,Gago, F.,Acebron, I.,de las Rivas, B.,Munoz, R.,Mancheno, J.M. (登録日: 2014-12-18, 公開日: 2015-07-15, 最終更新日: 2023-12-20)

主引用文献

Benavente, R.,Esteban-Torres, M.,Kohring, G.W.,Cortes-Cabrera, A.,Sanchez-Murcia, P.A.,Gago, F.,Acebron, I.,De Las Rivas, B.,Munoz, R.,Mancheno, J.M.
Enantioselective Oxidation of Galactitol 1-Phosphate by Galactitol-1-Phosphate 5-Dehydrogenase from Escherichia Coli
Acta Crystallogr.,Sect.D, 71:1540-, 2015

PubMed Abstract: Galactitol-1-phosphate 5-dehydrogenase (GPDH) is a polyol dehydrogenase that belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily. It catalyses the Zn(2+)- and NAD(+)-dependent stereoselective dehydrogenation of L-galactitol 1-phosphate to D-tagatose 6-phosphate. Here, three crystal structures of GPDH from Escherichia coli are reported: that of the open state of GPDH with Zn(2+) in the catalytic site and those of the closed state in complex with the polyols Tris and glycerol, respectively. The closed state of GPDH reveals no bound cofactor, which is at variance with the conformational transition of the prototypical mammalian liver alcohol dehydrogenase. The main intersubunit-contacting interface within the GPDH homodimer presents a large internal cavity that probably facilitates the relative movement between the subunits. The substrate analogue glycerol bound within the active site partially mimics the catalytically relevant backbone of galactitol 1-phosphate. The glycerol binding mode reveals, for the first time in the polyol dehydrogenases, a pentacoordinated zinc ion in complex with a polyol and also a strong hydrogen bond between the primary hydroxyl group and the conserved Glu144, an interaction originally proposed more than thirty years ago that supports a catalytic role for this acidic residue.

PubMed: 26143925
DOI: 10.1107/S1399004715009281

実験手法

X-RAY DIFFRACTION (1.74 Å)