4zv3: Difference between revisions

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==Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7==
==Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7==
<StructureSection load='4zv3' size='340' side='right' caption='[[4zv3]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='4zv3' size='340' side='right'caption='[[4zv3]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4zv3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZV3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4zv3]] is a 3 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=4ZV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZV3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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]] 3.1&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv3 PDBsum]</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=4zv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv3 OCA], [https://pdbe.org/4zv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zv3 RCSB], [https://www.ebi.ac.uk/pdbsum/4zv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zv3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
 
==See Also==
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Palmitoyl-CoA hydrolase]]
[[Category: Large Structures]]
[[Category: Forwood, J K]]
[[Category: Mus musculus]]
[[Category: Swarbrick, C M.D]]
[[Category: Forwood JK]]
[[Category: Double hotdog]]
[[Category: Swarbrick CMD]]
[[Category: Hydrolase]]
[[Category: Inflammation]]
[[Category: Thioesterase]]

Latest revision as of 11:24, 27 September 2023

Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7

Structural highlights

4zv3 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

See Also

References

  1. ↑ Kuramochi Y, Takagi-Sakuma M, Kitahara M, Emori R, Asaba Y, Sakaguchi R, Watanabe T, Kuroda J, Hiratsuka K, Nagae Y, Suga T, Yamada J. Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization. Brain Res Mol Brain Res. 2002 Jan 31;98(1-2):81-92. PMID:11834298

4zv3, resolution 3.10Å

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