8ait
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ait]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halopseudomonas_bauzanensis Halopseudomonas bauzanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIT FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ait]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halopseudomonas_bauzanensis Halopseudomonas bauzanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIT FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.24Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ait OCA], [https://pdbe.org/8ait PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ait RCSB], [https://www.ebi.ac.uk/pdbsum/8ait PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ait ProSAT]</span></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=8ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ait OCA], [https://pdbe.org/8ait PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ait RCSB], [https://www.ebi.ac.uk/pdbsum/8ait PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ait ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A031MKR8_9GAMM A0A031MKR8_9GAMM] | [https://www.uniprot.org/uniprot/A0A031MKR8_9GAMM A0A031MKR8_9GAMM] | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8ait" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of cutinase PbauzCut from Pseudomonas bauzanensis
| |||||||||||
