Yeast nicotinate-nucleotide pyrophosphorylase in complex with its ligand: Crystallization and Preliminary structural approaches

Pyridine-2,3-dicarboxylic acid which is a biologically potent molecule implicated in 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. S. cerevisiae NMnPP was obtained and diffracted to a resolution of 1.74 [A] and 1.99 [A] 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 the product binding and hexamer stabilization.