View source for 7yme


==Crystal structure of a PET hydrolase M9 variant from Cryptosporangium aurantiacum==
<StructureSection load='7yme' size='340' side='right'caption='[[7yme]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yme]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporangium_aurantiacum Cryptosporangium aurantiacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YME 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]] 1.5&#8491;</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=7yme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yme OCA], [https://pdbe.org/7yme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yme RCSB], [https://www.ebi.ac.uk/pdbsum/7yme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yme ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1M7II12_9ACTN A0A1M7II12_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Excessive polyethylene terephthalate (PET) waste causes a variety of problems. Extensive research focused on the development of superior PET hydrolases for PET biorecycling has been conducted. However, template enzymes employed in enzyme engineering mainly focused on IsPETase and leaf-branch compost cutinase, which exhibit mesophilic and thermophilic hydrolytic properties, respectively. Herein, we report a PET hydrolase from Cryptosporangium aurantiacum (CaPETase) that exhibits high thermostability and remarkable PET degradation activity at ambient temperatures. We uncover the crystal structure of CaPETase, which displays a distinct backbone conformation at the active site and residues forming the substrate binding cleft, compared with other PET hydrolases. We further develop a CaPETase(M9) variant that exhibits robust thermostability with a T(m) of 83.2 degrees C and 41.7-fold enhanced PET hydrolytic activity at 60 degrees C compared with CaPETase(WT). CaPETase(M9) almost completely decompose both transparent and colored post-consumer PET powder at 55 degrees C within half a day in a pH-stat bioreactor.

Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties.,Hong H, Ki D, Seo H, Park J, Jang J, Kim KJ Nat Commun. 2023 Jul 28;14(1):4556. doi: 10.1038/s41467-023-40233-w. PMID:37507390<ref>PMID:37507390</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yme" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Cryptosporangium aurantiacum]]
[[Category: Large Structures]]
[[Category: Hong H]]
[[Category: Ki D]]
[[Category: Kim K-J]]