@article{52351,
  author = {J. L. Avalos and I. Celic and S. Muhammad and M. S. Cosgrove and J. D. Boeke and C. Wolberger},
  title = {Structure of a Sir2 enzyme bound to an acetylated p53 peptide},
  abstract = {<p>Sir2 proteins are NAD(+)-dependent protein deacetylases that play key roles in transcriptional regulation, DNA repair, and life span regulation. The structure of an archaeal Sir2 enzyme, Sir2-Af2, bound to an acetylated p53 peptide reveals that the substrate binds in a cleft in the enzyme, forming an enzyme-substrate 0 sheet with two flanking strands in Sir2-Af2. The acetyllysine inserts into a conserved hydrophobic tunnel that contains the active site histidine. Comparison with other structures of Sir2 enzymes suggests that the apoenzyme undergoes a conformational change upon substrate binding. Based on the Sir2-Af2 substrate complex structure, mutations were made in the other A. fulgidus sirtuin, Sir2-Af1, that increased its affinity for the p53 peptide.</p>
},
  year = {2002},
  journal = {Molecular Cell},
  volume = {10},
  number = {3},
  pages = {523-535},
  month = {09/2002},
  isbn = {1097-2765},
  url = {http://www.cell.com/molecular-cell/abstract/S1097-2765(02)00628-7},
  language = {eng},
}