Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN

Item Type:	Article
Title:	Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN
Creators Name:	Werner, E. and Ziegler, M. and Lerner, F. and Schweiger, M. and Heinemann, U.
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.
Keywords:	Nicotinamide Mononucleotide Adenylyltransferase, Nicotinamide-Adenine Dinucleotide Biosynthesis, X-Ray Crystallography, Single-Wavelength Anomalous Dispersion, Protein Quaternary Structure
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Elsevier
Volume:	516
Number:	1-3
Page Range:	239-244
Date:	10 April 2002
Official Publication:	https://doi.org/10.1016/S0014-5793(02)02556-5
PubMed:	View item in PubMed

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