1X0X

Co-Structure of Homo Sapiens Glycerol-3-Phosphate Dehydrogenase 1 complex with NAD

Summary for 1X0X

• Entry DOI: 10.2210/pdb1x0x/pdb
• Related: 1WPQ 1X0V
• Descriptor: Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: nad, co-enzyme, gpd1, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P21695
• Total number of polymer chains: 1
• Total formula weight: 39163.74

Authors

Rao, Z.,Ou, X. (deposition date: 2005-03-31, release date: 2006-04-11, Last modification date: 2024-03-13)

Primary citation

Ou, X.,Ji, C.,Han, X.,Zhao, X.,Li, X.,Mao, Y.,Wong, L.L.,Bartlam, M.,Rao, Z.
Crystal Structures of Human Glycerol 3-phosphate Dehydrogenase 1 (GPD1)
J.Mol.Biol., 357:858-869, 2006

PubMed Abstract: 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.

PubMed: 16460752
DOI: 10.1016/j.jmb.2005.12.074

Experimental method

X-RAY DIFFRACTION (2.75 Å)