1ma3

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[[Image:1ma3.gif|left|200px]]
[[Image:1ma3.gif|left|200px]]
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{{Structure
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|PDB= 1ma3 |SIZE=350|CAPTION= <scene name='initialview01'>1ma3</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1ma3", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY=
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|GENE= SIR2-Af2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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|DOMAIN=
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{{STRUCTURE_1ma3| PDB=1ma3 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ma3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ma3 OCA], [http://www.ebi.ac.uk/pdbsum/1ma3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ma3 RCSB]</span>
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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'''
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[[Category: Muhammad, S.]]
[[Category: Muhammad, S.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
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[[Category: enzyme-substrate complex]]
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[[Category: Enzyme-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:48:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:25 2008''
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Revision as of 21:48, 2 May 2008

Image:1ma3.gif

Template:STRUCTURE 1ma3

Structure of a Sir2 enzyme bound to an acetylated p53 peptide


Overview

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.

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 Page seeded by OCA on Sat May 3 00:48:49 2008

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