4kgb

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'''Unreleased structure'''
 
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The entry 4kgb is ON HOLD until Paper Publication
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==Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster==
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<StructureSection load='4kgb' size='340' side='right'caption='[[4kgb]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4kgb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGB FirstGlance]. <br>
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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]] 2.64&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=4kgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgb OCA], [https://pdbe.org/4kgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgb RCSB], [https://www.ebi.ac.uk/pdbsum/4kgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SCOT_DROME SCOT_DROME] Key enzyme for ketone body catabolism (PubMed:24100554). Transfers the CoA moiety from succinate to acetoacetate (PubMed:24100554). Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).[UniProtKB:Q29551]<ref>PMID:24100554</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 A resolution and belonged to space group P212121, with unit-cell parameters a = 76.638, b = 101.921, c = 122.457 A, alpha = beta = gamma = 90 degrees . Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities.
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Authors: Wang, Y.C., Shi, Z.B., Zhang, M.
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Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.,Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1089-93., doi: 10.1107/S1744309113024986. Epub 2013 Sep 28. PMID:24100554<ref>PMID:24100554</ref>
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Description: Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster
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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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<div class="pdbe-citations 4kgb" style="background-color:#fffaf0;"></div>
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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: Drosophila melanogaster]]
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[[Category: Large Structures]]
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[[Category: Shi ZB]]
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[[Category: Wang YC]]
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[[Category: Zhang M]]

Current revision

Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster

PDB ID 4kgb

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