View source for 9hun


==Crystal structure of feruloyl esterase from Fusarium oxysporum G122S variant in complex with benzoic acid==
<StructureSection load='9hun' size='340' side='right'caption='[[9hun]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HUN 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]] 1.71&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=9hun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hun OCA], [https://pdbe.org/9hun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hun RCSB], [https://www.ebi.ac.uk/pdbsum/9hun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1D3S5H0_FUSOX A0A1D3S5H0_FUSOX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mono(2-hydroxyethyl) terephthalate (MHET) esterases (MHETases) are enzymes implicated in polyethylene terephthalate (PET) biodegradation. The present study elucidates the structural determinants that result in increased MHET degradation by a feruloyl esterase, which has been engineered to resemble the MHETase active site. The crystal structures of the variant in apo- and benzoic acid bound states reveal the changes induced by the introduced mutation, specifically the formation of a hydrogen bond and a trans to cis isomerization of a peptide bond in the vicinity of the catalytic site. Molecular dynamics simulations demonstrate the stabilization of the loop harboring the engineered residue, as well as an expansion of the substrate binding cleft, which would facilitate accommodation of a broader variety of substrates, indicative of a promiscuous biocatalyst.

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties.,Karampa P, Makryniotis K, Sousani TI, Topakas E, Daskalakis V, Dimarogona M FEBS Lett. 2026 Mar 8. doi: 10.1002/1873-3468.70322. PMID:41797379<ref>PMID:41797379</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hun" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusarium oxysporum]]
[[Category: Large Structures]]
[[Category: Dimarogona M]]
[[Category: Karampa P]]
[[Category: Makryniotis K]]
[[Category: Nikolaivits E]]
[[Category: Topakas E]]