4kgb: Difference between revisions
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==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=''> | ||
== 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> | |||
</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> | |||
<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='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'>[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> | |||
<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> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: 3-oxoacid CoA-transferase]] | [[Category: 3-oxoacid CoA-transferase]] | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Shi, Z B | [[Category: Shi, Z B]] | ||
[[Category: Wang, Y C | [[Category: Wang, Y C]] | ||
[[Category: Zhang, M | [[Category: Zhang, M]] | ||
[[Category: Ketone body catabolic process]] | [[Category: Ketone body catabolic process]] | ||
[[Category: Protein fold]] | [[Category: Protein fold]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
