Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN
Authors
- E. Werner
- M. Ziegler
- F. Lerner
- M. Schweiger
- U. Heinemann
Journal
- FEBS Letters
Citation
- FEBS Lett 516 (1-3): 239-244
Abstract
The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a major coenzyme in cellular redox reactions and involved in intracellular signaling, is catalyzed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex with nicotinamide mononucleotide was solved by the single-wavelength anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel {beta}-sheet with helices on both sides. Human NMNAT displays a different oligomerization compared to the archaeal enzyme. The protein-nicotinamide mononucleotide interaction pattern provides insight into ligand binding in the human enzyme.