3k6m

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[[Image:3k6m.png|left|200px]]
 
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==Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.==
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The line below this paragraph, containing "STRUCTURE_3k6m", creates the "Structure Box" on the page.
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<StructureSection load='3k6m' size='340' side='right'caption='[[3k6m]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3k6m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6M FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3k6m| PDB=3k6m | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6m OCA], [https://pdbe.org/3k6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6m RCSB], [https://www.ebi.ac.uk/pdbsum/3k6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SCOT1_PIG SCOT1_PIG] Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k6m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3k6m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic tissues. It catalyses the transfer of coenzyme A (CoA) from succinyl-CoA to acetoacetate with a classical ping-pong mechanism. There is biochemical evidence that the enzyme undergoes conformational changes during the reaction, but no domain movements have been reported in the available crystal structures. Here, a structure of pig heart SCOT refined at 1.5 A resolution is presented, showing that one of the four enzyme subunits in the crystallographic asymmetric unit has a molecule of glycerol bound in the active site; the glycerol molecule is hydrogen bonded to the conserved catalytic glutamate residue and is likely to occupy the cosubstrate-binding site. The binding of glycerol is associated with a substantial relative movement (a 13 degrees rotation) of two previously undefined domains that close around the substrate-binding site. The binding orientation of one of the cosubstrates, acetoacetate, is suggested based on the glycerol binding and the possibility that this dynamic domain movement is of functional importance is discussed.
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===Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.===
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The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.,Coker SF, Lloyd AJ, Mitchell E, Lewis GR, Coker AR, Shoolingin-Jordan PM Acta Crystallogr D Biol Crystallogr. 2010 Jul;66(Pt 7):797-805. Epub 2010 Jun 19. PMID:20606260<ref>PMID:20606260</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20606260}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3k6m" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20606260 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20606260}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3k6m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6M OCA].
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==Reference==
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<ref group="xtra">PMID:020606260</ref><references group="xtra"/>
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[[Category: 3-oxoacid CoA-transferase]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Coker, A R.]]
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[[Category: Coker AR]]
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[[Category: Coker, S.]]
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[[Category: Coker S]]
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[[Category: Lewis, G R.]]
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[[Category: Lewis GR]]
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[[Category: Lloyd, A.]]
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[[Category: Lloyd A]]
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[[Category: Mitchell, E.]]
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[[Category: Mitchell E]]
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[[Category: Shoolingin-Jordan, P.]]
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[[Category: Shoolingin-Jordan P]]
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[[Category: Coa transferase]]
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[[Category: Dynamic domain]]
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[[Category: Glycerol]]
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[[Category: Mitochondrion]]
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[[Category: Scot]]
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[[Category: Transferase]]
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[[Category: Transit peptide]]
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Current revision

Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.

PDB ID 3k6m

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