Insights into ligand binding and catalysis of a central step in NAD+ synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes
| Autor: | Saridakis V, Christendat D, Matthew Kimber, Dharamsi A, Am, Edwards, Ef, Pai |
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| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Binding Sites Sequence Homology Amino Acid Protein Conformation Methanobacterium Molecular Sequence Data Crystallography X-Ray Ligands NAD Catalysis Protein Structure Secondary Models Chemical Mutagenesis Catalytic Domain Mutation Chromatography Gel Mutagenesis Site-Directed Amino Acid Sequence Nicotinamide-Nucleotide Adenylyltransferase Cloning Molecular Protein Binding |
| Zdroj: | Europe PubMed Central |
| ISSN: | 0021-9258 |
| Popis: | Nicotinamide mononucleotide adenylyltransferase (NMNATase) catalyzes the linking of NMN(+) or NaMN(+) with ATP, which in all organisms is one of the common step in the synthesis of the ubiquitous coenzyme NAD(+), via both de novo and salvage biosynthetic pathways. The structure of Methanobacterium thermoautotrophicum NMNATase determined using multiwavelength anomalous dispersion phasing revealed a nucleotide-binding fold common to nucleotidyltransferase proteins. An NAD(+) molecule and a sulfate ion were bound in the active site allowing the identification of residues involved in product binding. In addition, the role of the conserved (16)HXGH(19) active site motif in catalysis was probed by mutagenic, enzymatic and crystallographic techniques, including the characterization of an NMN(+)/SO4(2-) complex of mutant H19A NMNATase. |
| Databáze: | OpenAIRE |
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