View source for 4upd


==Open conformation of O. piceae sterol esterase mutant I544W==
<StructureSection load='4upd' size='340' side='right'caption='[[4upd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4upd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ophiostoma_piceae Ophiostoma piceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UPD 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7P9:[(2R)-2-HEPTANOYLOXY-3-PHOSPHONOOXY-PROPYL]+NONANOATE'>7P9</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=4upd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upd OCA], [https://pdbe.org/4upd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4upd RCSB], [https://www.ebi.ac.uk/pdbsum/4upd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4upd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2TFW1_9PEZI Q2TFW1_9PEZI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sterol esterases are able to efficiently hydrolyze both sterol esters and triglycerides and to carry out synthesis reactions in the presence of organic solvents. Their high versatility makes them excellent candidates for biotechnological purposes. Sterol esterase from fungus Ophiostoma piceae (OPE) belongs to the family abH03.01 of the Candida rugosa lipase-like proteins. Crystal structures of OPE were solved in this study for the closed and open conformations. Enzyme activation involves a large displacement of the conserved lid, structural rearrangements of loop alpha16-alpha17, and formation of a dimer with a large opening. Three PEG molecules are placed in the active site, mimicking chains of the triglyceride substrate, demonstrating the position of the oxyanion hole and the three pockets that accommodate the sn-1, sn-2 and sn-3 fatty acids chains. One of them is an internal tunnel, connecting the active center with the outer surface of the enzyme 30A far from the catalytic Ser220. Based on our structural and biochemical results we propose a mechanism by which a great variety of different substrates can be hydrolyzed in OPE paving the way for the construction of new variants to improve the catalytic properties of these enzymes and their biotechnological applications.

Crystal structures of Ophiostoma piceae sterol esterase: Structural insights into activation mechanism and product release.,Gutierrez-Fernandez J, Vaquero ME, Prieto A, Barriuso J, Martinez MJ, Hermoso JA J Struct Biol. 2014 Sep;187(3):215-22. doi: 10.1016/j.jsb.2014.07.007. Epub 2014 , Aug 7. PMID:25108239<ref>PMID:25108239</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4upd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cholesterol esterase 3D structures|Cholesterol esterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ophiostoma piceae]]
[[Category: Barriuso J]]
[[Category: Gonzalez MJ]]
[[Category: Gutierrez-Fernandez J]]
[[Category: Hermoso JA]]
[[Category: Prieto A]]
[[Category: Vaquero ME]]