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Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT)

Item Type:Article
Title:Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT)
Creators Name:Werner, E. and Ziegler, M. and Lerner, F. and Schweiger, M. and Muller, Y.A. and Heinemann, U.
Abstract:Nicotinamide mononucleotide adenylyltransferase catalyses the final step in the synthesis of nicotinamide-adenine dinucleotide (NAD+) by transferring the adenylyl moiety of ATP to nicotinamide mononucleotide (NMN) with the release of pyrophosphate. The human enzyme was crystallized in the presence of NAD+. Crystals grew in the orthorhombic space group C2221, with unit-cell parameters a = 140.3, b = 235.5, c = 89.3 A, and diffract to a maximum resolution of 3.0 Å. Packing considerations suggest a trimer or higher multimer to be present in the asymmetric unit of the crystal. Two archaeal homologues have been described to form hexamers.
Keywords:Amino Acid Sequence, Amino Acid Sequence Homology, Crystallization, Molecular Cloning, Molecular Sequence Data, Nicotinamide-Nucleotide Adenylyltransferase, Protein Conformation, Non-U.S. Govt Support, X-Ray Crystallography
Source:Acta Crystallographica Section D
ISSN:0907-4449
Publisher:International Union of Crystallography (U.K.)
Volume:58
Number:1
Page Range:140-142
Date:1 January 2002
Official Publication:https://doi.org/10.1107/S0907444901017437
PubMed:View item in PubMed

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