Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN

FEBS Letters

Schweiger, Manfred¹  Heinemann, Udo²  Werner, Erik²  Ziegler, Mathias¹  Lerner, Felicitas¹ 

[1] Institute of Chemistry – Biochemistry, Free University of Berlin, Thielallee 63, D-14195 Berlin, Germany;Crystallography Group, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13092 Berlin, Germany

关键词: Nicotinamide mononucleotide adenylyltransferase;    Nicotinamide-adenine dinucleotide biosynthesis;    X-ray crystallography;    Single-wavelength anomalous dispersion;    Protein quaternary structure;    NMNAT;    nicotinamide mononucleotide adenylyltransferase;    NaMNAT;    nicotinate mononucleotide adenylyltransferase;    NAD+;    nicotinamide-adenine dinucleotide;    NMN;    nicotinamide mononucleotide;    NaAD;    deamido-NAD;    SAD;    single-wavelength anomalous dispersion;    NCS;    non-crystallographic symmetry;    SeMet;    selenomethionine;    r.m.s.d.;    root-mean-square deviation;   

DOI  :  10.1016/S0014-5793(02)02556-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel β-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.

【 授权许可】

Unknown