4uek

Galactitol-1-phosphate 5-dehydrogenase from E. coli with Tris within the active site.

spinqualitylabelsall models 4uek, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uek is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: TRS, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GATD_ECOLI Converts galactitol 1-phosphate to tagatose 6-phosphate. Publication Abstract from PubMed 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. Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli.,Benavente R, Esteban-Torres M, Kohring GW, Cortes-Cabrera A, Sanchez-Murcia PA, Gago F, Acebron I, de Las Rivas B, Munoz R, Mancheno JM Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1540-54. doi:, 10.1107/S1399004715009281. Epub 2015 Jun 30. PMID:26143925 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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