1ma3: Difference between revisions

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[[Image:1ma3.gif|left|200px]]
{{Seed}}
[[Image:1ma3.png|left|200px]]


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{{STRUCTURE_1ma3|  PDB=1ma3  |  SCENE=  }}  
{{STRUCTURE_1ma3|  PDB=1ma3  |  SCENE=  }}  


'''Structure of a Sir2 enzyme bound to an acetylated p53 peptide'''
===Structure of a Sir2 enzyme bound to an acetylated p53 peptide===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_12408821}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12408821 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12408821}}


==About this Structure==
==About this Structure==
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[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
[[Category: Enzyme-substrate complex]]
[[Category: Enzyme-substrate complex]]
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