1GZU

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

Replaces:  1GRY

Summary for 1GZU

• Entry DOI: 10.2210/pdb1gzu/pdb
• Related: 1GRY
• Descriptor: NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE (2 entities in total)
• Functional Keywords: transferase, nad biosynthesis, adenylyltransferase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 3
• Total formula weight: 101338.90

Authors

Werner, E.,Ziegler, M.,Lerner, F.,Schweiger, M.,Heinemann, U. (deposition date: 2002-06-06, release date: 2002-07-05, Last modification date: 2024-11-13)

Primary citation

Werner, E.,Ziegler, M.,Lerner, F.,Schweiger, M.,Heinemann, U.
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.
FEBS Lett., 516:239-244, 2002

PubMed 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.

PubMed: 11959140
DOI: 10.1016/S0014-5793(02)02556-5

Experimental method

X-RAY DIFFRACTION (2.9 Å)