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3hlk
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3hlk is ON HOLD Authors: Mandel,C.R., Tweel,B., Tong,L. Description: Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) ''Page...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)== | |
| + | <StructureSection load='3hlk' size='340' side='right'caption='[[3hlk]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3hlk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLK FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACOT2, PTE2, PTE2A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </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=3hlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hlk OCA], [https://pdbe.org/3hlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hlk RCSB], [https://www.ebi.ac.uk/pdbsum/3hlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hlk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/ACOT2_HUMAN ACOT2_HUMAN]] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs.<ref>PMID:10944470</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hlk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hlk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acyl-CoA thioesterases (ACOTs) catalyze the hydrolysis of CoA esters to free CoA and carboxylic acids and have important functions in lipid metabolism and other cellular processes. Type I ACOTs are found only in animals and contain an alpha/beta hydrolase domain, through currently no structural information is available on any of these enzymes. We report here the crystal structure at 2.1A resolution of human mitochondrial ACOT2, a type I enzyme. The structure contains two domains, N and C domains. The C domain has the alpha/beta hydrolase fold, with the catalytic triad Ser294-His422-Asp388. The N domain contains a seven-stranded beta-sandwich, which has some distant structural homologs in other proteins. The active site is located in a large pocket at the interface between the two domains. The structural information has significant relevance for other type I ACOTs and related enzymes. | ||
| - | + | Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2).,Mandel CR, Tweel B, Tong L Biochem Biophys Res Commun. 2009 Aug 7;385(4):630-3. Epub 2009 Jun 2. PMID:19497300<ref>PMID:19497300</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3hlk" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Palmitoyl-CoA hydrolase]] | ||
| + | [[Category: Mandel, C R]] | ||
| + | [[Category: Tong, L]] | ||
| + | [[Category: Tweel, B]] | ||
| + | [[Category: Alpha/beta hydrolase]] | ||
| + | [[Category: Alternative splicing]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Mitochondrion]] | ||
| + | [[Category: Polymorphism]] | ||
| + | [[Category: Serine esterase]] | ||
| + | [[Category: Transit peptide]] | ||
Current revision
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
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