View source for 8air


==Crystal structure of cutinase RgCutII from Rhizobacter gummiphilus==
<StructureSection load='8air' size='340' side='right'caption='[[8air]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8air]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobacter_gummiphilus Rhizobacter gummiphilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIR 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]] 1.08&#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=8air FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8air OCA], [https://pdbe.org/8air PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8air RCSB], [https://www.ebi.ac.uk/pdbsum/8air PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8air ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1W6L438_9BURK A0A1W6L438_9BURK] 
<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 8air" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizobacter gummiphilus]]
[[Category: Allen MD]]
[[Category: McGeehan JE]]
[[Category: Pickford AR]]
[[Category: Zahn M]]