Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT)
| Autor: | Manfred Schweiger, Felicitas Lerner, Udo Heinemann, Erik Werner, Mathias Ziegler, Yves A. Muller |
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| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Sequence Homology Amino Acid Chemistry Stereochemistry Protein Conformation Molecular Sequence Data Trimer General Medicine Crystallography X-Ray Pyrophosphate Crystallography chemistry.chemical_compound Enzyme Protein structure Structural Biology Moiety Humans Orthorhombic crystal system NAD+ kinase Amino Acid Sequence Nicotinamide-Nucleotide Adenylyltransferase Cloning Molecular Crystallization Nicotinamide mononucleotide |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 58(Pt 1) |
| ISSN: | 0907-4449 |
| Popis: | 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 C222(1), with unit-cell parameters a = 140.3, b = 235.5, c = 89.3 A, and diffract to a maximum resolution of 3.0 A. 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. |
| Databáze: | OpenAIRE |
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