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Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN
Author(s) -
Werner Erik,
Ziegler Mathias,
Lerner Felicitas,
Schweiger Manfred,
Heinemann Udo
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02556-5
Subject(s) - nicotinamide mononucleotide , random hexamer , chemistry , nad+ kinase , nicotinamide adenine dinucleotide , enzyme , adenosylcobalamin , biochemistry , stereochemistry , cofactor
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.