3uuf
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3uuf is ON HOLD Authors: Xu, T.T., Xu, J.X., Hou, S.L., Liu, J.S. Description: Crystal structure of mono-and diacylglycerol lipase from Malassezia ...) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa== | |
| + | <StructureSection load='3uuf' size='340' side='right'caption='[[3uuf]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3uuf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Malassezia_globosa_CBS_7966 Malassezia globosa CBS 7966]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UUF 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]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3uuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uuf OCA], [https://pdbe.org/3uuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uuf RCSB], [https://www.ebi.ac.uk/pdbsum/3uuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uuf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LIP1_MALGO LIP1_MALGO] Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids (PubMed:17460728, PubMed:18000048). Shows activity against monoglyceride and diglyceride substrates, but not triglyceride substrates and does not exhibit regio-selective production of diacylglycerols (PubMed:17460728, PubMed:22750000, PubMed:25837472, PubMed:25955297, PubMed:26239010, PubMed:26365206, PubMed:27130210). Able to hydrolyze diacylglycerols such as distearin, dilinolein, dipalmitoylglycerol and dipalmitolein (PubMed:27130210). Cleaves oleic acid from 1,2 isomers of diolein on both the 1 and the 2 position of the glycerol backbone, resulting mainly in free fatty acids but no monoolein is detected (PubMed:27130210). Shows activity on monoolein and liberates mostly free fatty acids, but can also perform the reverse reaction and produce diolein (PubMed:27130210).<ref>PMID:17460728</ref> <ref>PMID:18000048</ref> <ref>PMID:22750000</ref> <ref>PMID:25837472</ref> <ref>PMID:25955297</ref> <ref>PMID:26239010</ref> <ref>PMID:26365206</ref> <ref>PMID:27130210</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Most lipases contain a lid domain to shield the hydrophobic binding site from the water environment. The lid, mostly in helical form, can undergo a conformational change to expose the active cleft during the interfacial activation. Here we report the crystal structures of Malassezia globosa LIP1 (SMG1) at 1.45 and 2.60A resolution in two crystal forms. The structures present SMG1 in its closed form, with a novel lid in loop conformation. SMG1 is one of the few members in the fungal lipase family that has been found to be strictly specific for mono- and diacylglycerol. To date, the mechanism for this substrate specificity remains largely unknown. To investigate the substrate binding properties, we built a model of SMG1 in open conformation. Based on this model, we found that the two bulky hydrophobic residues adjacent to the catalytic site and the N-terminal hinge region of the lid both may act as steric hindrances for triacylglycerols binding. These unique structural features of SMG1 will provide a better understanding on the substrate specificity of mono- and diacylglycerol lipases and a platform for further functional study of this enzyme. | ||
| - | + | Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity.,Xu T, Liu L, Hou S, Xu J, Yang B, Wang Y, Liu J J Struct Biol. 2012 Mar 29. PMID:22484238<ref>PMID:22484238</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3uuf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Lipase 3D Structures|Lipase 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Malassezia globosa CBS 7966]] | ||
| + | [[Category: Hou S]] | ||
| + | [[Category: Liu J]] | ||
| + | [[Category: Xu J]] | ||
| + | [[Category: Xu T]] | ||
Current revision
Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa
| |||||||||||
