View source for 8ais


==Crystal structure of cutinase PsCut from Pseudomonas saudimassiliensis==
<StructureSection load='8ais' size='340' side='right'caption='[[8ais]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ais]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_saudimassiliensis Pseudomonas saudimassiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIS 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]] 1.56&#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></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=8ais FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ais OCA], [https://pdbe.org/8ais PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ais RCSB], [https://www.ebi.ac.uk/pdbsum/8ais PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ais ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A078MGG8_9PSED A0A078MGG8_9PSED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). PETase from Ideonella sakaiensis (IsPETase) is capable of PET hydrolysis under mild conditions but suffers from concentration-dependent inhibition. In this study, this inhibition is found to be dependent on incubation time, the solution conditions, and PET surface area. Furthermore, this inhibition is evident in other mesophilic PET-degrading enzymes to varying degrees, independent of the level of PET depolymerization activity. The inhibition has no clear structural basis, but moderately thermostable IsPETase variants exhibit reduced inhibition, and the property is completely absent in the highly thermostable HotPETase, previously engineered by directed evolution, which simulations suggest results from reduced flexibility around the active site. This work highlights a limitation in applying natural mesophilic hydrolases for PET hydrolysis and reveals an unexpected positive outcome of engineering these enzymes for enhanced thermostability.

Concentration-Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering.,Avilan L, Lichtenstein BR, Konig G, Zahn M, Allen MD, Oliveira L, Clark M, Bemmer V, Graham R, Austin HP, Dominick G, Johnson CW, Beckham GT, McGeehan JE, Pickford AR ChemSusChem. 2023 Apr 21;16(8):e202202277. doi: 10.1002/cssc.202202277. Epub 2023 , Mar 23. PMID:36811288<ref>PMID:36811288</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ais" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas saudimassiliensis]]
[[Category: Allen MD]]
[[Category: McGeehan JE]]
[[Category: Pickford AR]]
[[Category: Zahn M]]