2cy9: Difference between revisions

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==Crystal structure of thioesterase superfamily member2 from Mus musculus==
==Crystal structure of thioesterase superfamily member2 from Mus musculus==
<StructureSection load='2cy9' size='340' side='right' caption='[[2cy9]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
<StructureSection load='2cy9' size='340' side='right'caption='[[2cy9]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cy9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CY9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cy9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CY9 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.72&#8491;</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=2cy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy9 OCA], [http://pdbe.org/2cy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cy9 RCSB], [http://www.ebi.ac.uk/pdbsum/2cy9 PDBsum], [http://www.topsan.org/Proteins/RSGI/2cy9 TOPSAN]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2cy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy9 OCA], [https://pdbe.org/2cy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cy9 RCSB], [https://www.ebi.ac.uk/pdbsum/2cy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cy9 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cy9 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ACO13_MOUSE ACO13_MOUSE]] 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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis.<ref>PMID:19405909</ref> <ref>PMID:24072708</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cy9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cy9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2cy9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Large Structures]]
[[Category: Hosaka, T]]
[[Category: Mus musculus]]
[[Category: Kishishita, S]]
[[Category: Hosaka T]]
[[Category: Murayama, K]]
[[Category: Kishishita S]]
[[Category: Structural genomic]]
[[Category: Murayama K]]
[[Category: Shirouzu, M]]
[[Category: Shirouzu M]]
[[Category: Yokoyama, S]]
[[Category: Yokoyama S]]
[[Category: Hydrolase]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rsgi]]
[[Category: Thioesterase superfamily member 2]]