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TitleMechanism of Sirtuin Inhibition by Nicotinamide: Altering the NAD(+) Cosubstrate Specificity of a Sir2 Enzyme.
Journal, issue, pagesMol. Cell, Vol. 17, Page 855-868, Year 2005
Publish dateDec 21, 2004 (structure data deposition date)
AuthorsAvalos, J.L. / Bever, K.M. / Wolberger, C.
External linksMol. Cell / PubMed:15780941
MethodsX-ray diffraction
Resolution1.4 - 2.4 Å
Structure data

PDB-1yc2:
Sir2Af2-NAD-ADPribose-nicotinamide
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1yc5:
Sir2-p53 peptide-nicotinamide
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-NCA:
NICOTINAMIDE / medication*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-2PE:
NONAETHYLENE GLYCOL / precipitant*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-APR:
ADENOSINE-5-DIPHOSPHORIBOSE

ChemComp-HOH:
WATER

Source
  • archaeoglobus fulgidus (archaea)
  • thermotoga maritima (bacteria)
KeywordsHYDROLASE / sir2 / sirtuin / nicotinamide / NAD / ADPribose / ternary complex / sir2Tm / SirT1 / p53

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