BioDesign 2022; 10(4): 73-78
Published online December 30, 2022
© Korean Society for Structural Biology
Tae Gyun Kim1,†,*, Taek Hun Kwon2,†, Hyojeong Choi1, Min-Kyung Park1, JoongBae Park1, In Gyeong Chae1 and Hyun-Jung An1
1R&D Planning Team, Vaccine Commercialization Center, Gyeongbuk Institute for Bio Industry, Andong 36618, Republic of Korea
2Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston 77030, TX, USA
Correspondence to: *firstname.lastname@example.org
†These authors contributed equally to this work.
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.