Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT).
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.
Werner
Erik
E
Crystallography Group, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, D-13092 Berlin, Germany.
Ziegler
Mathias
M
Lerner
Felicitas
F
Schweiger
Manfred
M
Muller
Yves A
YA
Heinemann
Udo
U
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D009612:Nicotinamide-Nucleotide Adenylyltransferase / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D009612:Nicotinamide-Nucleotide Adenylyltransferase