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The Structure of a Eukaryotic Nicotinic Acid Phosphoribosyltransferase Reveals Structural Heterogeneity among Type II PRTases
- Source :
- Structure. 13:1385-1396
- Publication Year :
- 2005
- Publisher :
- Elsevier BV, 2005.
-
Abstract
- SummaryNicotinamide adenine dinucleotide (NAD) is an essential cofactor for cellular redox reactions and can act as an important substrate in numerous biological processes. As a result, nature has evolved multiple biosynthetic pathways to meet this high chemical demand. In Saccharomyces cerevisiae, the NAD salvage pathway relies on the activity of nicotinic acid phosphoribosyltransferase (NAPRTase), a member of the phosphoribosyltransferase (PRTase) superfamily. Here, we report the structure of a eukaryotic (yeast) NAPRTase at 1.75 Å resolution (locus name: YOR209C, gene name: NPT1). The structure reveals a two-domain fold that resembles the architecture of quinolinic acid phosphoribosyltransferases (QAPRTases), but with completely different dispositions that provide evidence for structural heterogeneity among the Type II PRTases. The identification of a third domain in NAPRTases provides a structural basis and possible mechanism for the functional modulation of this family of enzymes by ATP.
- Subjects :
- chemistry.chemical_classification
Genetics
Protein Folding
Binding Sites
biology
Saccharomyces cerevisiae
Nicotinamide adenine dinucleotide
NAD
biology.organism_classification
Cofactor
Protein Structure, Tertiary
chemistry.chemical_compound
Adenosine Triphosphate
Protein structure
Enzyme
Biochemistry
chemistry
Structural Biology
biology.protein
Phosphoribosyltransferase
Transferase
Pentosyltransferases
NAD+ kinase
Molecular Biology
Subjects
Details
- ISSN :
- 09692126
- Volume :
- 13
- Database :
- OpenAIRE
- Journal :
- Structure
- Accession number :
- edsair.doi.dedup.....2fcf2e512a6f6e43641401e51077b842