1ma3: Difference between revisions

Revision as of 23:32, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ma3.png

Template:STRUCTURE 1ma3

Structure of a Sir2 enzyme bound to an acetylated p53 peptideStructure of a Sir2 enzyme bound to an acetylated p53 peptide

Template:ABSTRACT PUBMED 12408821

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 23:32:11 2008

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OCA

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