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==Crystal structure of human Monoacylglycerol Lipase ABHD6 in complex with oleic acid and octyl glucoside==
==Crystal structure of human Monoacylglycerol Lipase ABHD6 in complex with oleic acid and octyl glucoside==
<StructureSection load='7ots' size='340' side='right'caption='[[7ots]]' scene=''>
<StructureSection load='7ots' size='340' side='right'caption='[[7ots]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OTS FirstGlance]. <br>
<table><tr><td colspan='2'>[[7ots]] 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=7OTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OTS FirstGlance]. <br>
</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=7ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ots OCA], [https://pdbe.org/7ots PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ots RCSB], [https://www.ebi.ac.uk/pdbsum/7ots PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ots ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABHD6 ([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/Acylglycerol_lipase Acylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.23 3.1.1.23] </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=7ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ots OCA], [https://pdbe.org/7ots PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ots RCSB], [https://www.ebi.ac.uk/pdbsum/7ots PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ots ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ABHD6_HUMAN ABHD6_HUMAN]] Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015).[UniProtKB:Q8R2Y0]<ref>PMID:22969151</ref> <ref>PMID:26491015</ref> 
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acylglycerol lipase]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Miallau L]]
[[Category: Miallau, L]]
[[Category: Nawrotek A]]
[[Category: Nawrotek, A]]
[[Category: Talagas A]]
[[Category: Talagas, A]]
[[Category: Vuillard L]]
[[Category: Vuillard, L]]
[[Category: 2-ag signalling]]
[[Category: 2-arachidonoylglycerol hydrolase]]
[[Category: Alpha/beta-hydrolase domain containing 6]]
[[Category: Endocannabinoid system]]
[[Category: Hydrolase]]
[[Category: Monoacylglycerol lipase abhd6]]
[[Category: Nervous system]]

Revision as of 09:38, 25 August 2021

Crystal structure of human Monoacylglycerol Lipase ABHD6 in complex with oleic acid and octyl glucosideCrystal structure of human Monoacylglycerol Lipase ABHD6 in complex with oleic acid and octyl glucoside

Structural highlights

7ots is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:ABHD6 (HUMAN)
Activity:Acylglycerol lipase, with EC number 3.1.1.23
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ABHD6_HUMAN] Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015).[UniProtKB:Q8R2Y0][1] [2]

References

  1. Navia-Paldanius D, Savinainen JR, Laitinen JT. Biochemical and pharmacological characterization of human alpha/beta-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12). J Lipid Res. 2012 Nov;53(11):2413-24. doi: 10.1194/jlr.M030411. Epub 2012 Sep 11. PMID:22969151 doi:http://dx.doi.org/10.1194/jlr.M030411
  2. Pribasnig MA, Mrak I, Grabner GF, Taschler U, Knittelfelder O, Scherz B, Eichmann TO, Heier C, Grumet L, Kowaliuk J, Romauch M, Holler S, Anderl F, Wolinski H, Lass A, Breinbauer R, Marsche G, Brown JM, Zimmermann R. alpha/beta Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate. J Biol Chem. 2015 Dec 11;290(50):29869-81. doi: 10.1074/jbc.M115.669168. Epub, 2015 Oct 21. PMID:26491015 doi:http://dx.doi.org/10.1074/jbc.M115.669168

7ots, resolution 1.79Å

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