Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Crystallography, X-Ray
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Humans
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Macromolecular Substances
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Methanobacterium / enzymology
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Methanobacterium / genetics
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Molecular Sequence Data
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Nicotinamide Mononucleotide / chemistry*
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Nicotinamide-Nucleotide Adenylyltransferase / chemistry*
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Nicotinamide-Nucleotide Adenylyltransferase / genetics
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Protein Conformation
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Protein Structure, Secondary
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Protein Subunits
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Sequence Homology, Amino Acid
Substances
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Macromolecular Substances
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Protein Subunits
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Recombinant Proteins
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Nicotinamide Mononucleotide
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Nicotinamide-Nucleotide Adenylyltransferase
Associated data
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PDB/1B6T
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PDB/1EJ2
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PDB/1F9A
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PDB/1GZU
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PDB/1HYB
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PDB/1K4K
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PDB/1K4M
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PDB/1KAM
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PDB/1KAQ
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PDB/1KKU
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PDB/1KQN
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PDB/1KQO
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PDB/1KR2