Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.
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Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.
FEBS Lett. 2002 Apr 10;516(1-3):239-44.
- PubMed ID
- 11959140 [ View in PubMed]
- 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.