4kgb
From Proteopedia
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| - | {{STRUCTURE_4kgb| PDB=4kgb | SCENE= }} | ||
| - | ===Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster=== | ||
| - | {{ABSTRACT_PUBMED_24100554}} | ||
| - | == | + | ==Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster== |
| - | [[http://www.uniprot.org/uniprot/ | + | <StructureSection load='4kgb' size='340' side='right'caption='[[4kgb]], [[Resolution|resolution]] 2.64Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.64Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | + | <div class="pdbe-citations 4kgb" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Shi ZB]] |
| - | [[Category: | + | [[Category: Wang YC]] |
| - | [[Category: | + | [[Category: Zhang M]] |
| - | + | ||
| - | + | ||
Current revision
Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster
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