期刊
MOLECULAR CELL
卷 10, 期 3, 页码 523-535出版社
CELL PRESS
DOI: 10.1016/S1097-2765(02)00628-7
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资金
- NCI NIH HHS [CA84760-02] Funding Source: Medline
- NIGMS NIH HHS [GM62385] Funding Source: Medline
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.
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