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- W2134629557 abstract "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 β sheet with two flanking strands in Sir2-Af2. The acetyl-lysine 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." @default.
- W2134629557 created "2016-06-24" @default.
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- W2134629557 date "2002-09-01" @default.
- W2134629557 modified "2023-10-11" @default.
- W2134629557 title "Structure of a Sir2 Enzyme Bound to an Acetylated p53 Peptide" @default.
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- W2134629557 doi "https://doi.org/10.1016/s1097-2765(02)00628-7" @default.
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