1gzu
From Proteopedia
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Revision as of 13:19, 30 October 2007
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CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN
Overview
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.
About this Structure
1GZU is a [Single protein] structure of sequence from [Homo sapiens] with NMN as [ligand]. This structure superseeds the now removed PDB entry 1GRY. Active as [Nicotinamide-nucleotide adenylyltransferase], with EC number [2.7.7.1]. Structure known Active Site: NMA. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN., Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U, FEBS Lett. 2002 Apr 10;516(1-3):239-44. PMID:11959140
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