Structure of a Sir2 Enzyme Bound to an Acetylated p53 Peptide
Copyright policy )Structure of a Sir2 Enzyme Bound to an Acetylated p53 Peptide
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 beta 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.
- Johns Hopkins Medicine United States
- Johns Hopkins University School of Medicine United States
Models, Molecular, Binding Sites, Molecular Structure, Archaeal Proteins, Molecular Sequence Data, Acetylation, Cell Biology, Crystallography, X-Ray, Protein Structure, Tertiary, Archaeoglobus fulgidus, Humans, Sirtuins, Amino Acid Sequence, Tumor Suppressor Protein p53, Peptides, Molecular Biology, Sequence Alignment, Protein Binding
Models, Molecular, Binding Sites, Molecular Structure, Archaeal Proteins, Molecular Sequence Data, Acetylation, Cell Biology, Crystallography, X-Ray, Protein Structure, Tertiary, Archaeoglobus fulgidus, Humans, Sirtuins, Amino Acid Sequence, Tumor Suppressor Protein p53, Peptides, Molecular Biology, Sequence Alignment, Protein Binding
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