1wpq

Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone

spinqualitylabelsall models 1wpq, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wpq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 13P, NAD, SO4 Activity: Glycerol-3-phosphate dehydrogenase (NAD(+)), with EC number 1.1.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [GPDA_HUMAN] Defects in GPD1 are a cause of hypertriglyceridemia, transient infantile (HTGTI) [MIM:614480]. An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes the reversible biological conversion of dihydroxyacetone (DHAP) to glycerol-3-phosphate. The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein with glutathione S-transferase. Here we report the apoenzyme structure of GPD1 determined by multiwavelength anomalous diffraction phasing, and other complex structures with small molecules (NAD+ and DHAP) by the molecular replacement method. This enzyme structure is organized into two distinct domains, the N-terminal eight-stranded beta-sheet sandwich domain and the C-terminal helical substrate-binding domain. An electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analyses. In addition, the inhibitory effects of zinc and sulfate on GPDHs are assayed and discussed. Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1).,Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. PMID:16460752 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycerol-3-phosphate dehydrogenase 3D structures

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