FEBS Letters | |
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN | |
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
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