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3hlk

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{{Seed}}
 
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[[Image:3hlk.jpg|left|200px]]
 
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<!--
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==Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)==
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The line below this paragraph, containing "STRUCTURE_3hlk", creates the "Structure Box" on the page.
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<StructureSection load='3hlk' size='340' side='right'caption='[[3hlk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_3hlk| PDB=3hlk | SCENE= }}
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<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>
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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=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>
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</table>
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== Function ==
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[[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hlk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)===
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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>
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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 3hlk" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19497300}}, adds the Publication Abstract to the page
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19497300 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19497300}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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3HLK is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLK OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:19497300</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
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[[Category: Palmitoyl-CoA hydrolase]]
[[Category: Palmitoyl-CoA hydrolase]]
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[[Category: Mandel, C R.]]
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[[Category: Mandel, C R]]
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[[Category: Tong, L.]]
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[[Category: Tong, L]]
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[[Category: Tweel, B.]]
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[[Category: Tweel, B]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alternative splicing]]
[[Category: Alternative splicing]]
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[[Category: Serine esterase]]
[[Category: Serine esterase]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 09:07:38 2009''
 

Current revision

Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)

PDB ID 3hlk

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