Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN

FEBS Lett. 2002 Apr 10;516(1-3):239-44. doi: 10.1016/s0014-5793(02)02556-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Humans
  • Macromolecular Substances
  • Methanobacterium / enzymology
  • Methanobacterium / genetics
  • Molecular Sequence Data
  • Nicotinamide Mononucleotide / chemistry*
  • Nicotinamide-Nucleotide Adenylyltransferase / chemistry*
  • Nicotinamide-Nucleotide Adenylyltransferase / genetics
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Subunits
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sequence Homology, Amino Acid


  • Macromolecular Substances
  • Protein Subunits
  • Recombinant Proteins
  • Nicotinamide Mononucleotide
  • Nicotinamide-Nucleotide Adenylyltransferase

Associated data

  • PDB/1B6T
  • PDB/1EJ2
  • PDB/1F9A
  • PDB/1GZU
  • PDB/1HYB
  • PDB/1K4K
  • PDB/1K4M
  • PDB/1KAM
  • PDB/1KAQ
  • PDB/1KKU
  • PDB/1KQN
  • PDB/1KQO
  • PDB/1KR2