View source for 3uue


==Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa==
<StructureSection load='3uue' size='340' side='right'caption='[[3uue]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uue]] 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=3UUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UUE 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=3uue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uue OCA], [https://pdbe.org/3uue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uue RCSB], [https://www.ebi.ac.uk/pdbsum/3uue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uue ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8PUY1_MALGO A8PUY1_MALGO] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3uue" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Malassezia globosa CBS 7966]]
[[Category: Hou S]]
[[Category: Liu J]]
[[Category: Xu J]]
[[Category: Xu T]]