Yeast nicotinate-nucleotide pyrophosphorylase in complex with ligand: crystallization and preliminary structural approaches

Yeast nicotinate-nucleotide pyrophosphorylase in complex with ligand: crystallization and preliminary structural approaches

Pyridine-2,3-dicarboxylic acid which is a biologically potent molecule implicated in the neurodegenerative environment is catalyzed by nicotinate-nucleotide pyrophosphorylase (NMnPP) to produce a precursor molecule, nicotinate mononucleotide (NMn), of de novo biosynthesis of the coenzyme nicotinamide adenine dinucleotide (NAD+). The protein preparation, crystallization, and preliminary structural features of full-length enzyme in complex with product reactant suggest that yeast NMnPP acts as stable hexamer formation. Crystals of S. cerevisiae NMnPP were obtained and diffracted to a resolution of 1.74 Å and 1.99 Å for apo and complex forms, belonged to the trigonal symmetry group R32 in the unit-cell parameters of a = b = 155.313, c = 67.507 and a = b = 155.091, c = 69.204, respectively. Based on our comparison of eukaryotic NMnPP structures in the apo and complex forms, we propose functional and structural investigation for product binding and hexamer stabilization.