Abstract
ABSTRACTPyridine-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), ofde novobiosynthesis 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. cerevisiaeNMnPP was obtained and diffracted to a resolution of 1.74 Å and 1.99 Å for apo and complex forms, belonged to the trigonal symmetry groupR32 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.
Publisher
Cold Spring Harbor Laboratory