7c4d: Difference between revisions

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-'''Unreleased structure'''
-The entry 7c4d is ON HOLD
+==Marine microorganism esterase==
+<StructureSection load='7c4d' size='340' side='right'caption='[[7c4d]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7c4d]] 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=7C4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C4D 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]] 2.03&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c4d OCA], [https://pdbe.org/7c4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c4d RCSB], [https://www.ebi.ac.uk/pdbsum/7c4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c4d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A2S1GUX0_9BACT A0A2S1GUX0_9BACT]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Lipolytic enzymes are essential biocatalysts in food processing as well as pharmaceutical and pesticide industries, catalyzing the cleavage of ester bonds in a variety of acyl chain substrates. Here, we report the crystal structure of an esterase from the deep-sea hydrothermal vent of the East Pacific Rise (EprEst). The X-ray structure of EprEst in complex with the ligand, acetate, has been determined at 2.03 A resolution. The structure reveals a unique spatial arrangement and orientation of the helix cap domain and alpha/beta hydrolase domain, which form a substrate pocket with preference for short-chain acyl groups. Molecular docking analysis further demonstrated that the active site pocket could accommodate p-nitrophenyl (pNP) carboxyl ligands of varying lengths (&lt;/=6 C atoms), with pNP-butyrate ester predicted to have the highest binding affinity. Additionally, the semirational design was conducted to improve the thermostability of EprEst by enzyme engineering based on the established structure and multiple sequence alignment. A mutation, K114P, introduced in the hinge region of the esterase, which displayed increased thermostability and enzyme activity. Collectively, the structural and functional data obtained herein could be used as basis for further protein engineering to ultimately expand the scope of industrial applications of marine-derived lipolytic enzymes.
-Authors:
+Structural Insights into a Novel Esterase from the East Pacific Rise and Its Improved Thermostability by a Semirational Design.,Zhu C, Chen Y, Isupov MN, Littlechild JA, Sun L, Liu X, Wang Q, Gong H, Dong P, Zhang N, Wu Y J Agric Food Chem. 2021 Jan 27;69(3):1079-1090. doi: 10.1021/acs.jafc.0c06338., Epub 2021 Jan 14. PMID:33445864<ref>PMID:33445864</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7c4d" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Uncultured bacterium]]
+[[Category: Isupov MN]]
+[[Category: Wu YK]]
+[[Category: Zhu CH]]