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    FEBS Lett. 2002 Apr 10;516(1-3):239-44.

    Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.

    Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U.

    Crystallography Group, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13092, Berlin, Germany. ewe@mdc-berlin.de

    Erratum in:

    • FEBS Lett 2002 Jul 17;523(1-3):254-5.

    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.

    PMID: 11959140 [PubMed - indexed for MEDLINE]

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