View source for 5hc0


==Structure of esterase Est22 with p-nitrophenol==
<StructureSection load='5hc0' size='340' side='right'caption='[[5hc0]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HC0 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]] 1.4&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</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=5hc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hc0 OCA], [https://pdbe.org/5hc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hc0 RCSB], [https://www.ebi.ac.uk/pdbsum/5hc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hc0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H6BDX1_9BACT H6BDX1_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hormone sensitive lipase (HSL) catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol, thus playing key roles in energy homeostasis. However, the application of HSL serving as a pharmaceutical target and an industrial biocatalyst is largely hampered due to the lack of high-resolution structural information. Here we report biochemical properties and crystal structures of a novel HSL homologue esterase Est22 from a deep-sea metagenomic library. Est22 prefers short acyl chain esters and has a very high activity with substrate p-nitrophenyl butyrate. The crystal structures of wild type and mutated Est22 with its product p-nitrophenol are solved with resolutions ranging from 1.4 A to 2.43 A. The Est22 exhibits a alpha/beta-hydrolase fold consisting with a catalytic domain and a substrate-recognizing cap domain. Residues Ser188, Asp287, and His317 comprise the catalytic triad in the catalytic domain. The p-nitrophenol molecule occupies the substrate binding pocket and forms hydrogen bonds with adjacent residues Gly108, Gly109, and Gly189. Est22 exhibits a dimeric form in solution, whereas mutants D287A and H317A change to polymeric form, which totally abolished its enzymatic activities. Our study provides insights into the catalytic mechanism of HSL family esterase and facilitates the understanding for further industrial and biotechnological applications of esterases.

Structural insights of a hormone sensitive lipase homologue Est22.,Huang J, Huo YY, Ji R, Kuang S, Ji C, Xu XW, Li J Sci Rep. 2016 Jun 22;6:28550. doi: 10.1038/srep28550. PMID:27328716<ref>PMID:27328716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hc0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured bacterium]]
[[Category: Huang J]]
[[Category: Li J]]