1ma3

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[[Image:1ma3.gif|left|200px]]
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{{STRUCTURE_1ma3| PDB=1ma3 | SCENE= }}
{{STRUCTURE_1ma3| PDB=1ma3 | SCENE= }}
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'''Structure of a Sir2 enzyme bound to an acetylated p53 peptide'''
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===Structure of a Sir2 enzyme bound to an acetylated p53 peptide===
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==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.
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(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.]]
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[[Category: Enzyme-substrate complex]]
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Revision as of 20:32, 2 July 2008

Image:1ma3.png

Template:STRUCTURE 1ma3

Structure of a Sir2 enzyme bound to an acetylated p53 peptide

Template:ABSTRACT PUBMED 12408821

About this Structure

1MA3 is a Protein complex structure of sequences from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Structure of a Sir2 enzyme bound to an acetylated p53 peptide., Avalos JL, Celic I, Muhammad S, Cosgrove MS, Boeke JD, Wolberger C, Mol Cell. 2002 Sep;10(3):523-35. PMID:12408821

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