View source for 9j57


==ESTS1 phthalate ester degrading esterase from Sulfobacillus acidophilus in complex with paranitrophenyl butyrate==
<StructureSection load='9j57' size='340' side='right'caption='[[9j57]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9j57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfobacillus_acidophilus_DSM_10332 Sulfobacillus acidophilus DSM 10332]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9J57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9J57 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=R5C:(4-nitrophenyl)+butanoate'>R5C</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=9j57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9j57 OCA], [https://pdbe.org/9j57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9j57 RCSB], [https://www.ebi.ac.uk/pdbsum/9j57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9j57 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G8TV28_SULAD G8TV28_SULAD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phthalate diesters are important pollutants and act as endocrine disruptors. While certain bacterial esterases have been identified for phthalate diesters degradation to monoesters, their structural and mechanistic characteristics remain largely unexplored. Here, we highlight the potential of the thermostable and pH-tolerant EstS1 esterase from Sulfobacillus acidophilus DSM10332 to degrade high molecular weight bis(2-ethylhexyl) phthalate (DEHP) by combining biophysical and biochemical approaches along with high-resolution EstS1 crystal structures of the apo form and with bound substrates, products, and their analogs to elucidate its mechanism. The catalytic tunnel mediates entry and exit of the substrate and product, respectively. The centralized Ser-His-Asp triad performs catalysis by a bi-bi ping-pong mechanism, forming a tetrahedral intermediate. Mutagenesis analysis showed that the Met207Ala mutation abolished DEHP binding at the active site, confirming its essential role in supporting catalysis. These findings underscore EstS1 as a promising tool for advancing technologies aimed at phthalate diesters biodegradation.

Mechanistic and structural insights into EstS1 esterase: A potent broad-spectrum phthalate diester degrading enzyme.,Verma S, Choudhary S, Amith Kumar K, Mahto JK, Vamsi K AK, Mishra I, Prakash VB, Sircar D, Tomar S, Kumar Sharma A, Singla J, Kumar P Structure. 2024 Nov 28:S0969-2126(24)00496-9. doi: 10.1016/j.str.2024.11.006. PMID:39642872<ref>PMID:39642872</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9j57" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfobacillus acidophilus DSM 10332]]
[[Category: Kumar P]]
[[Category: Verma S]]