7osb: Difference between revisions
New page: '''Unreleased structure''' The entry 7osb is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal Structure of a Double Mutant PETase (S238F/W159H) from Ideonella sakaiensis== | |||
<StructureSection load='7osb' size='340' side='right'caption='[[7osb]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OSB 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]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=7osb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7osb OCA], [https://pdbe.org/7osb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7osb RCSB], [https://www.ebi.ac.uk/pdbsum/7osb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7osb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
There is keen interest to develop new technologies to recycle the plastic poly(ethylene terephthalate) (PET). To this end, the use of PET-hydrolyzing enzymes has shown promise for PET deconstruction to its monomers, terephthalate (TPA) and ethylene glycol (EG). Here, we compare the Ideonella sakaiensis PETase wild-type enzyme to a previously reported improved variant (W159H/S238F). We compare the thermostability of each enzyme and describe a 1.45 A resolution structure of the mutant, highlighting changes in the substrate binding cleft compared to the wild-type enzyme. Subsequently, the performance of the wild-type and variant enzyme was compared as a function of temperature, substrate morphology, and reaction mixture composition. These studies show that reaction temperature has the strongest influence on performance between the two enzymes. We also show that both enzymes achieve higher levels of PET conversion for substrates with moderate crystallinity relative to amorphous substrates. Finally, we assess the impact of product accumulation on reaction progress for the hydrolysis of both PET and bis(2-hydroxyethyl) terephthalate (BHET). Each enzyme displays different inhibition profiles to mono(2-hydroxyethyl) terephthalate (MHET) and TPA, while both are sensitive to inhibition by EG. Overall, this study highlights the importance of reaction conditions, substrate selection, and product accumulation for catalytic performance of PET-hydrolyzing enzymes, which have implications for enzyme screening in the development of enzyme- based polyester recycling. | |||
Comparative performance of PETase as a function of reaction conditions, substrate properties, and product accumulation.,Erickson E, Shakespeare TJ, Bratti F, Buss BL, Graham R, Hawkins MA, Konig G, Michener WE, Miscall J, Ramirez KJ, Rorrer NA, Zahn M, Pickford AR, McGeehan JE, Beckham G ChemSusChem. 2021 Sep 29. doi: 10.1002/cssc.202101932. PMID:34587366<ref>PMID:34587366</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7osb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Allen MD]] | |||
[[Category: McGeehan JE]] | |||
[[Category: Shakespeare TJ]] | |||
[[Category: Zahn M]] | |||
Latest revision as of 12:03, 17 October 2024
Crystal Structure of a Double Mutant PETase (S238F/W159H) from Ideonella sakaiensisCrystal Structure of a Double Mutant PETase (S238F/W159H) from Ideonella sakaiensis
Structural highlights
Publication Abstract from PubMedThere is keen interest to develop new technologies to recycle the plastic poly(ethylene terephthalate) (PET). To this end, the use of PET-hydrolyzing enzymes has shown promise for PET deconstruction to its monomers, terephthalate (TPA) and ethylene glycol (EG). Here, we compare the Ideonella sakaiensis PETase wild-type enzyme to a previously reported improved variant (W159H/S238F). We compare the thermostability of each enzyme and describe a 1.45 A resolution structure of the mutant, highlighting changes in the substrate binding cleft compared to the wild-type enzyme. Subsequently, the performance of the wild-type and variant enzyme was compared as a function of temperature, substrate morphology, and reaction mixture composition. These studies show that reaction temperature has the strongest influence on performance between the two enzymes. We also show that both enzymes achieve higher levels of PET conversion for substrates with moderate crystallinity relative to amorphous substrates. Finally, we assess the impact of product accumulation on reaction progress for the hydrolysis of both PET and bis(2-hydroxyethyl) terephthalate (BHET). Each enzyme displays different inhibition profiles to mono(2-hydroxyethyl) terephthalate (MHET) and TPA, while both are sensitive to inhibition by EG. Overall, this study highlights the importance of reaction conditions, substrate selection, and product accumulation for catalytic performance of PET-hydrolyzing enzymes, which have implications for enzyme screening in the development of enzyme- based polyester recycling. Comparative performance of PETase as a function of reaction conditions, substrate properties, and product accumulation.,Erickson E, Shakespeare TJ, Bratti F, Buss BL, Graham R, Hawkins MA, Konig G, Michener WE, Miscall J, Ramirez KJ, Rorrer NA, Zahn M, Pickford AR, McGeehan JE, Beckham G ChemSusChem. 2021 Sep 29. doi: 10.1002/cssc.202101932. PMID:34587366[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||