View source for 5gw8


==Crystal structure of a putative DAG-like lipase (MgMDL2) from Malassezia globosa==
<StructureSection load='5gw8' size='340' side='right'caption='[[5gw8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gw8]] is a 2 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=5GW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GW8 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</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=5gw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw8 OCA], [https://pdbe.org/5gw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gw8 RCSB], [https://www.ebi.ac.uk/pdbsum/5gw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8PUY5_MALGO A8PUY5_MALGO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipases play an important role in physiological metabolism and diseases, and also have multiple industrial applications. Rational modification of lipase specificity may increase the commercial utility of this group of enzymes, but is hindered by insufficient mechanistic understanding. Here, we report the 2.0 A resolution crystal structure of a mono- and di-acylglycerols lipase from Malassezia globosa (MgMDL2). Interestingly, residues Phe278 and Glu282 were found to involve in substrate recognition because mutation on each residue led to convert MgMDL2 to a triacylglycerol (TAG) lipase. The Phe278Ala and Glu282Ala mutants also acquired ability to synthesize TAGs by esterification of glycerol and fatty acids. By in silicon analysis, steric hindrance of these residues seemed to be key factors for the altered substrate specificity. Our work may shed light on understanding the unique substrate selectivity mechanism of mono- and di-acylglycerols lipases, and provide a new insight for engineering biocatalysts with desired catalytic behaviors for biotechnological application.

Malassezia globosa MgMDL2 lipase: Crystal structure and rational modification of substrate specificity.,Lan D, Xu H, Xu J, Dubin G, Liu J, Iqbal Khan F, Wang Y Biochem Biophys Res Commun. 2017 Jun 24;488(2):259-265. doi:, 10.1016/j.bbrc.2017.04.103. Epub 2017 Apr 20. PMID:28433636<ref>PMID:28433636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gw8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Malassezia globosa CBS 7966]]
[[Category: Liu J]]
[[Category: Xu H]]
[[Category: Xu J]]