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| | <StructureSection load='4zwn' size='340' side='right'caption='[[4zwn]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='4zwn' size='340' side='right'caption='[[4zwn]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zwn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZWN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zwn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZWN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.491Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylglycerol_lipase Acylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.23 3.1.1.23] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zwn OCA], [http://pdbe.org/4zwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zwn RCSB], [http://www.ebi.ac.uk/pdbsum/4zwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zwn ProSAT]</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=4zwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zwn OCA], [https://pdbe.org/4zwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zwn RCSB], [https://www.ebi.ac.uk/pdbsum/4zwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zwn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MGLL_YEAST MGLL_YEAST]] Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA).<ref>PMID:19529773</ref> <ref>PMID:20554061</ref> | + | [https://www.uniprot.org/uniprot/MGLL_YEAST MGLL_YEAST] Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA).<ref>PMID:19529773</ref> <ref>PMID:20554061</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Lipase|Lipase]] | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acylglycerol lipase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aschauer, P]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gruber, K]] | + | [[Category: Aschauer P]] |
| - | [[Category: Oberer, M]] | + | [[Category: Gruber K]] |
| - | [[Category: Rengachari, S]] | + | [[Category: Oberer M]] |
| - | [[Category: Alpha/beta hydrolase]]
| + | [[Category: Rengachari S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Monoacylglycerol lipase]]
| + | |
| - | [[Category: Monoglyceride lipase]]
| + | |
| - | [[Category: Serine hydrolase]]
| + | |
| Structural highlights
Function
MGLL_YEAST Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA).[1] [2]
Publication Abstract from PubMed
Monoglyceride lipases (MGLs) are a group of alpha/beta-hydrolases that catalyze the hydrolysis of monoglycerides (MGs) into free fatty acids and glycerol. This reaction serves different physiological functions, namely in the last step of phospholipid and triglyceride degradation, in mammalian endocannabinoid and arachidonic acid metabolism, and in detoxification processes in microbes. Previous crystal structures of MGLs from humans and bacteria revealed conformational plasticity in the cap region of this protein and gave insight into substrate binding. In this study, we present the structure of a MGL from Saccharomyces cerevisiae called Yju3p in its free form and in complex with a covalently bound substrate analog mimicking the tetrahedral intermediate of MG hydrolysis. These structures reveal a high conservation of the overall shape of the MGL cap region and also provide evidence for conformational changes in the cap of Yju3p. The complex structure reveals that, despite the high structural similarity, Yju3p seems to have an additional opening to the substrate binding pocket at a different position compared to human and bacterial MGL. Substrate specificities towards MGs with saturated and unsaturated alkyl chains of different lengths were tested and revealed highest activity towards MG containing a C18:1 fatty acid.
Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p.,Aschauer P, Rengachari S, Lichtenegger J, Schittmayer M, Das KM, Mayer N, Breinbauer R, Birner-Gruenberger R, Gruber CC, Zimmermann R, Gruber K, Oberer M Biochim Biophys Acta. 2016 May;1861(5):462-70. doi: 10.1016/j.bbalip.2016.02.005., Epub 2016 Feb 9. PMID:26869448[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muccioli GG, Sia A, Muchowski PJ, Stella N. Genetic manipulation of palmitoylethanolamide production and inactivation in Saccharomyces cerevisiae. PLoS One. 2009 Jun 16;4(6):e5942. doi: 10.1371/journal.pone.0005942. PMID:19529773 doi:http://dx.doi.org/10.1371/journal.pone.0005942
- ↑ Heier C, Taschler U, Rengachari S, Oberer M, Wolinski H, Natter K, Kohlwein SD, Leber R, Zimmermann R. Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae. Biochim Biophys Acta. 2010 Sep;1801(9):1063-71. doi:, 10.1016/j.bbalip.2010.06.001. Epub 2010 Jun 8. PMID:20554061 doi:http://dx.doi.org/10.1016/j.bbalip.2010.06.001
- ↑ Aschauer P, Rengachari S, Lichtenegger J, Schittmayer M, Das KM, Mayer N, Breinbauer R, Birner-Gruenberger R, Gruber CC, Zimmermann R, Gruber K, Oberer M. Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p. Biochim Biophys Acta. 2016 May;1861(5):462-70. doi: 10.1016/j.bbalip.2016.02.005., Epub 2016 Feb 9. PMID:26869448 doi:http://dx.doi.org/10.1016/j.bbalip.2016.02.005
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