3gls: Difference between revisions

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-[[Image:3gls.png|left|200px]]
-{{STRUCTURE_3gls|  PDB=3gls  |  SCENE=  }}
+==Crystal Structure of Human SIRT3==
+<StructureSection load='3gls' size='340' side='right'caption='[[3gls]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3gls]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GLS 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]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3gls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gls OCA], [https://pdbe.org/3gls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gls RCSB], [https://www.ebi.ac.uk/pdbsum/3gls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gls ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SIR3_HUMAN SIR3_HUMAN] NAD-dependent protein deacetylase. Activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.<ref>PMID:16788062</ref> <ref>PMID:18680753</ref> <ref>PMID:18794531</ref> <ref>PMID:19535340</ref>
+== 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/gl/3gls_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3gls ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SIRT3 is a major mitochondrial NAD(+)-dependent protein deacetylase playing important roles in regulating mitochondrial metabolism and energy production and has been linked to the beneficial effects of exercise and caloric restriction. SIRT3 is emerging as a potential therapeutic target to treat metabolic and neurological diseases. We report the first sets of crystal structures of human SIRT3, an apo-structure with no substrate, a structure with a peptide containing acetyl lysine of its natural substrate acetyl-CoA synthetase 2, a reaction intermediate structure trapped by a thioacetyl peptide, and a structure with the dethioacetylated peptide bound. These structures provide insights into the conformational changes induced by the two substrates required for the reaction, the acetylated substrate peptide and NAD(+). In addition, the binding study by isothermal titration calorimetry suggests that the acetylated peptide is the first substrate to bind to SIRT3, before NAD(+). These structures and biophysical studies provide key insight into the structural and functional relationship of the SIRT3 deacetylation activity.
-===Crystal Structure of Human SIRT3===
+Crystal structures of human SIRT3 displaying substrate-induced conformational changes.,Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB J Biol Chem. 2009 Sep 4;284(36):24394-405. Epub 2009 Jun 16. PMID:19535340<ref>PMID:19535340</ref>
-{{ABSTRACT_PUBMED_19535340}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3gls" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[3gls]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GLS OCA].
+*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019535340</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bemis, J E.]]
+[[Category: Large Structures]]
-[[Category: Cai, J.]]
+[[Category: Bemis JE]]
-[[Category: Dai, H.]]
+[[Category: Cai J]]
-[[Category: Jiang, Y.]]
+[[Category: Dai H]]
-[[Category: Jin, L.]]
+[[Category: Jiang Y]]
-[[Category: Jirousek, M R.]]
+[[Category: Jin L]]
-[[Category: Mao, C.]]
+[[Category: Jirousek MR]]
-[[Category: Milne, J C.]]
+[[Category: Mao C]]
-[[Category: Peng, H.]]
+[[Category: Milne JC]]
-[[Category: Perni, R B.]]
+[[Category: Peng H]]
-[[Category: Wei, W.]]
+[[Category: Perni RB]]
-[[Category: Westphal, C H.]]
+[[Category: Wei W]]
-[[Category: Apo structure]]
+[[Category: Westphal CH]]
-[[Category: Hydrolase]]
-[[Category: Metal-binding]]
-[[Category: Mitochondrion]]
-[[Category: Nad]]
-[[Category: Nad dependent deacetylase]]
-[[Category: Sirtuin]]
-[[Category: Transit peptide]]