9kl9: Difference between revisions
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==crystal structure of a mutant Poly(Ethylene terephthalate) hydrolase== | |||
<StructureSection load='9kl9' size='340' side='right'caption='[[9kl9]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9kl9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacterium_HR29 Bacterium HR29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KL9 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]] 2.9Å</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=9kl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kl9 OCA], [https://pdbe.org/9kl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kl9 RCSB], [https://www.ebi.ac.uk/pdbsum/9kl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kl9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2H5Z9R5_UNCXX A0A2H5Z9R5_UNCXX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymatic PET depolymerization represents a promising approach for establishing a circular economy for PET plastics. Nonetheless, limitations in enzyme activity persist as significant challenges to its industrial application. In this research, the backbone structure of the beta6-beta7 loop for PET hydrolase Bhr-PETase derived from the thermophilic bacterium HR29 was reconstructed by introducing double mutations (H218N/F222M), resulting in variant Bhr-NMT with high thermal stability (T(m) = 92.9 degrees C) and 87% increase in activity. Moreover, the loop reconstruction mutations are transplanted into the engineered PET hydrolases LCC-ICCG and Kubu-P(M12), resulting variants LCC-ICCG-NM (T(m) = 92.4 degrees C) and Kubu-P(M12)-NM (T(m) = 92.9 degrees C). Under high substrate concentration (165 g kg(-1)) and an enzyme loading of 0.5 mg(enzyme) g(PET)(-1), the designed variants Bhr-NMT, LCC-ICCG-NM, and Kubu-P(M12)-NM achieve an overall conversion of 93%, 90%, and 94%, respectively, outperforming the benchmark LCC-ICCG (85%). Notably, under reduced enzyme loading (0.3 mg(enzyme) g(PET)(-1)), Kubu-P(M12)-NM still reaches an overall conversion of 91%, which is significantly superior to benchmarks Kubu-P(M12) (83%) and LCC-ICCG (71%). Overall, the engineered PET hydrolases demonstrate significant potential for industrial PET waste recycling. | |||
Computational loop reconstruction based design of efficient PET hydrolases.,Wang H, Cun Y, Wang M, Du X, Yang Z, Wang H, Zhang J, Wang P, Feng Y, Zhu Y Commun Biol. 2025 Jun 17;8(1):934. doi: 10.1038/s42003-025-08364-6. PMID:40527955<ref>PMID:40527955</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9kl9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacterium HR29]] | |||
[[Category: Large Structures]] | |||
[[Category: Du XY]] | |||
[[Category: Feng Y]] | |||
[[Category: Wang H]] | |||
Latest revision as of 05:53, 1 October 2025
crystal structure of a mutant Poly(Ethylene terephthalate) hydrolase
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