1x0v
From Proteopedia
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Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1
Overview
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.
About this Structure
1X0V is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Glycerol-3-phosphate dehydrogenase (NAD(+)), with EC number 1.1.1.8 Full crystallographic information is available from OCA.
Reference
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
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