2v1o: Difference between revisions

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[[Image:2v1o.png|left|200px]]


{{STRUCTURE_2v1o| PDB=2v1o | SCENE= }}
==Crystal structure of N-terminal domain of acyl-CoA thioesterase 7==
<StructureSection load='2v1o' size='340' side='right'caption='[[2v1o]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2v1o]] is a 6 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=2V1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=2v1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1o OCA], [https://pdbe.org/2v1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1o RCSB], [https://www.ebi.ac.uk/pdbsum/2v1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACH_MOUSE BACH_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. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.<ref>PMID:11834298</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/v1/2v1o_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=2v1o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acyl-CoA thioesterases (Acots) catalyze the hydrolysis of fatty acyl-CoA to free fatty acid and CoA and thereby regulate lipid metabolism and cellular signaling. We present a comprehensive structural and functional characterization of mouse acyl-CoA thioesterase 7 (Acot7). Whereas prokaryotic homologues possess a single thioesterase domain, mammalian Acot7 contains a pair of domains in tandem. We determined the crystal structures of both the N- and C-terminal domains of the mouse enzyme, and inferred the structure of the full-length enzyme using a combination of chemical cross-linking, mass spectrometry, and molecular modeling. The quaternary arrangement in Acot7 features a trimer of hotdog fold dimers. Both domains of Acot7 are required for activity, but only one of two possible active sites in the dimer is functional. Asn-24 and Asp-213 (from N- and C-domains, respectively) were identified as the catalytic residues through site-directed mutagenesis. An enzyme with higher activity than wild-type Acot7 was obtained by mutating the residues in the nonfunctional active site. Recombinant Acot7 was shown to have the highest activity toward arachidonoyl-CoA, suggesting a function in eicosanoid metabolism. In line with the proposal, Acot7 was shown to be highly expressed in macrophages and up-regulated by lipopolysaccharide. Overexpression of Acot7 in a macrophage cell line modified the production of prostaglandins D2 and E2. Together, the results link the molecular and cellular functions of Acot7 and identify the enzyme as a candidate drug target in inflammatory disease.


===CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF ACYL-COA THIOESTERASE 7===
Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation.,Forwood JK, Thakur AS, Guncar G, Marfori M, Mouradov D, Meng W, Robinson J, Huber T, Kellie S, Martin JL, Hume DA, Kobe B Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10382-7. Epub 2007 Jun 11. PMID:17563367<ref>PMID:17563367</ref>


{{ABSTRACT_PUBMED_17563367}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2v1o" style="background-color:#fffaf0;"></div>
[[2v1o]] is a 6 chain structure of [[Thioesterase]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1O OCA].


==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017563367</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Forwood, J K.]]
[[Category: Forwood JK]]
[[Category: Guncar, G.]]
[[Category: Guncar G]]
[[Category: Huber, T.]]
[[Category: Huber T]]
[[Category: Hume, D A.]]
[[Category: Hume DA]]
[[Category: Kellie, S.]]
[[Category: Kellie S]]
[[Category: Kobe, B.]]
[[Category: Kobe B]]
[[Category: Marfori, M.]]
[[Category: Marfori M]]
[[Category: Martin, J L.]]
[[Category: Martin JL]]
[[Category: Meng, W N.]]
[[Category: Meng WN]]
[[Category: Mouradov, D.]]
[[Category: Mouradov D]]
[[Category: Robinson, J.]]
[[Category: Robinson J]]
[[Category: Thakur, A S.]]
[[Category: Thakur AS]]
[[Category: Acot7]]
[[Category: Acyl-coa thioesterase 7]]
[[Category: Domain duplication]]
[[Category: Hotdog domain]]
[[Category: Hydrolase]]
[[Category: Macrophage]]
[[Category: Protein structure]]
[[Category: Serine esterase]]
Retrieved from "https://proteopedia.org/2v1o"