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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.


DOI

doi:10.1016/S0014-5793(02)02556-5