Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT)

Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):140-2. doi: 10.1107/s0907444901017437. Epub 2001 Dec 21.


Nicotinamide mononucleotide adenylyltransferase catalyses the final step in the synthesis of nicotinamide-adenine dinucleotide (NAD(+)) by transferring the adenylyl moiety of ATP to nicotinamide mononucleotide (NMN) with the release of pyrophosphate. The human enzyme was crystallized in the presence of NAD(+). Crystals grew in the orthorhombic space group C222(1), with unit-cell parameters a = 140.3, b = 235.5, c = 89.3 A, and diffract to a maximum resolution of 3.0 A. Packing considerations suggest a trimer or higher multimer to be present in the asymmetric unit of the crystal. Two archaeal homologues have been described to form hexamers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Nicotinamide-Nucleotide Adenylyltransferase / chemistry*
  • Nicotinamide-Nucleotide Adenylyltransferase / genetics
  • Protein Conformation
  • Sequence Homology, Amino Acid


  • Nicotinamide-Nucleotide Adenylyltransferase