1ope

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[[Image:1ope.jpg|left|200px]]
 
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{{Structure
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==Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART==
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|PDB= 1ope |SIZE=350|CAPTION= <scene name='initialview01'>1ope</scene>, resolution 2.50&Aring;
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<StructureSection load='1ope' size='340' side='right'caption='[[1ope]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene>
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<table><tr><td colspan='2'>[[1ope]] is a 2 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=1OPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPE FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase 3-oxoacid CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.5 2.8.3.5]
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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]] 2.5&#8491;</td></tr>
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|GENE= OXCT OR SCOT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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}}
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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=1ope FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ope OCA], [https://pdbe.org/1ope PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ope RCSB], [https://www.ebi.ac.uk/pdbsum/1ope PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ope ProSAT]</span></td></tr>
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</table>
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'''Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART'''
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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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==Overview==
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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/op/1ope_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=1ope 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 ==
Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the acetoacetate in ketone bodies by transferring the CoA group from succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In the reaction, a glutamate residue at the active site of the enzyme forms a thioester bond with CoA and in this form the enzyme is subject to autolytic fragmentation. The crystal structure of pig heart SCOT has been solved and refined to 1.7 A resolution in a new crystal form. The structure shows the active-site glutamate residue in a conformation poised for autolytic fragmentation, with its side chain accepting one hydrogen bond from Asn281 and another from its own amide N atom. However, the conformation of this glutamate side chain would have to change for the residues that are conserved in the CoA transferases (Gln99, Gly386 and Ala387) to participate in stabilizing the tetrahedral transition states of the catalytic mechanism. The structures of a deletion mutant in two different crystal forms were also solved.
Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the acetoacetate in ketone bodies by transferring the CoA group from succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In the reaction, a glutamate residue at the active site of the enzyme forms a thioester bond with CoA and in this form the enzyme is subject to autolytic fragmentation. The crystal structure of pig heart SCOT has been solved and refined to 1.7 A resolution in a new crystal form. The structure shows the active-site glutamate residue in a conformation poised for autolytic fragmentation, with its side chain accepting one hydrogen bond from Asn281 and another from its own amide N atom. However, the conformation of this glutamate side chain would have to change for the residues that are conserved in the CoA transferases (Gln99, Gly386 and Ala387) to participate in stabilizing the tetrahedral transition states of the catalytic mechanism. The structures of a deletion mutant in two different crystal forms were also solved.
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==About this Structure==
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Structure of the CoA transferase from pig heart to 1.7 A resolution.,Coros AM, Swenson L, Wolodko WT, Fraser ME Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1717-25. Epub 2004, Sep 23. PMID:15388917<ref>PMID:15388917</ref>
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1OPE is a [[Single protein]] structure of 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=1OPE OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the CoA transferase from pig heart to 1.7 A resolution., Coros AM, Swenson L, Wolodko WT, Fraser ME, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1717-25. Epub 2004, Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15388917 15388917]
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</div>
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[[Category: 3-oxoacid CoA-transferase]]
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<div class="pdbe-citations 1ope" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Coros, A M.]]
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[[Category: Coros AM]]
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[[Category: Fraser, M E.]]
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[[Category: Fraser ME]]
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[[Category: Swenson, L.]]
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[[Category: Swenson L]]
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[[Category: Wolodko, W T.]]
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[[Category: Wolodko WT]]
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[[Category: HG]]
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[[Category: K]]
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[[Category: alpha/beta protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:54 2008''
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Current revision

Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART

PDB ID 1ope

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