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| | ==Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster== | | ==Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster== |
| - | <StructureSection load='4kgb' size='340' side='right' caption='[[4kgb]], [[Resolution|resolution]] 2.64Å' scene=''> | + | <StructureSection load='4kgb' size='340' side='right'caption='[[4kgb]], [[Resolution|resolution]] 2.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kgb]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KGB FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG1140, Dmel_CG1140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kgb RCSB], [http://www.ebi.ac.uk/pdbsum/4kgb PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9W058_DROME Q9W058_DROME]] 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 (By similarity).[PIRNR:PIRNR000858] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4kgb" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-oxoacid CoA-transferase]] | |
| | [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
| - | [[Category: Shi, Z B]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, Y C]] | + | [[Category: Shi ZB]] |
| - | [[Category: Zhang, M]] | + | [[Category: Wang YC]] |
| - | [[Category: Ketone body catabolic process]] | + | [[Category: Zhang M]] |
| - | [[Category: Protein fold]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
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][1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN. Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster. 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 doi:http://dx.doi.org/10.1107/S1744309113024986
- ↑ Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN. Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster. 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 doi:http://dx.doi.org/10.1107/S1744309113024986
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