1NQO

Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate

Summary for 1NQO

• Entry DOI: 10.2210/pdb1nqo/pdb
• Related: 1NPT 1NQ5 1NQA
• Descriptor: Glyceraldehyde 3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, GLYCERALDEHYDE-3-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: glycolysis, oxidoreductase, nad
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm: P00362
• Total number of polymer chains: 4
• Total formula weight: 147233.87

Authors

Didierjean, C.,Corbier, C.,Fatih, M.,Favier, F.,Boschi-Muller, S.,Branlant, G.,Aubry, A. (deposition date: 2003-01-22, release date: 2003-04-22, Last modification date: 2023-08-16)

Primary citation

Didierjean, C.,Corbier, C.,Fatih, M.,Favier, F.,Boschi-Muller, S.,Branlant, G.,Aubry, A.
Crystal structure of two ternary complexes of phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus with NAD and D-Glyceraldehyde-3-Phosphate
J.Biol.Chem., 278:12968-12976, 2003

PubMed Abstract: The crystal structure of the phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus was solved in complex with its cofactor, NAD, and its physiological substrate, D-glyceraldehyde 3-phosphate (D-G3P). To isolate a stable ternary complex, the nucleophilic residue of the active site, Cys(149), was substituted with alanine or serine. The C149A and C149S GAPDH ternary complexes were obtained by soaking the crystals of the corresponding binary complexes (enzyme.NAD) in a solution containing G3P. The structures of the two binary and the two ternary complexes are presented. The D-G3P adopts the same conformation in the two ternary complexes. It is bound in a non-covalent way, in the free aldehyde form, its C-3 phosphate group being positioned in the P(s) site and not in the P(i) site. Its C-1 carbonyl oxygen points toward the essential His(176), which supports the role proposed for this residue along the two steps of the catalytic pathway. Arguments are provided that the structures reported here are representative of a productive enzyme.NAD.D-G3P complex in the ground state (Michaelis complex).

PubMed: 12569100
DOI: 10.1074/jbc.M211040200

Experimental method

X-RAY DIFFRACTION (2.01 Å)