1ope: Difference between revisions
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<StructureSection load='1ope' size='340' side='right'caption='[[1ope]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1ope' size='340' side='right'caption='[[1ope]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ope]] is a 2 chain structure with sequence from [ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<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> | |||
<tr id=' | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sus scrofa]] | ||
[[Category: Coros | [[Category: Coros AM]] | ||
[[Category: Fraser | [[Category: Fraser ME]] | ||
[[Category: Swenson | [[Category: Swenson L]] | ||
[[Category: Wolodko | [[Category: Wolodko WT]] | ||
Latest revision as of 12:30, 16 August 2023
Deletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEARTDeletion mutant of SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART
Structural highlights
FunctionSCOT1_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSuccinyl-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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