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New page: left|200px<br /> <applet load="1ma3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ma3, resolution 2.0Å" /> '''Structure of a Sir2 ...
 
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[[Image:1ma3.gif|left|200px]]<br />
<applet load="1ma3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ma3, resolution 2.0&Aring;" />
'''Structure of a Sir2 enzyme bound to an acetylated p53 peptide'''<br />


==Overview==
==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.
<StructureSection load='1ma3' size='340' side='right'caption='[[1ma3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ma3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MA3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ma3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ma3 OCA], [https://pdbe.org/1ma3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ma3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ma3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ma3 ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/1ma3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ma3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Disease==
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<ref>PMID:12408821</ref>
Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Breast cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Colorectal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Histiocytoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Li-Fraumeni syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Multiple malignancy syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Nasopharyngeal carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Osteosarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Pancreatic cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Thyroid carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1MA3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with ZN and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MA3 OCA].
</div>
 
<div class="pdbe-citations 1ma3" style="background-color:#fffaf0;"></div>
==Reference==
== References ==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12408821 12408821]
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Protein complex]]
[[Category: Homo sapiens]]
[[Category: Avalos, J.L.]]
[[Category: Large Structures]]
[[Category: Boeke, J.D.]]
[[Category: Avalos JL]]
[[Category: Celic, I.]]
[[Category: Boeke JD]]
[[Category: Cosgrove, M.S.]]
[[Category: Celic I]]
[[Category: Muhammad, S.]]
[[Category: Cosgrove MS]]
[[Category: Wolberger, C.]]
[[Category: Muhammad S]]
[[Category: MES]]
[[Category: Wolberger C]]
[[Category: ZN]]
[[Category: enzyme-substrate complex]]
 
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Latest revision as of 00:14, 21 November 2024

Structure of a Sir2 enzyme bound to an acetylated p53 peptide

1ma3, resolution 2.00Å

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