7vpa: Difference between revisions
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==Crystal structure of Ple629 from marine microbial consortium== | ==Crystal structure of Ple629 from marine microbial consortium== | ||
<StructureSection load='7vpa' size='340' side='right'caption='[[7vpa]]' scene=''> | <StructureSection load='7vpa' size='340' side='right'caption='[[7vpa]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VPA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7vpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Marinobacter Unclassified Marinobacter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VPA FirstGlance]. <br> | ||
</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=7vpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vpa OCA], [https://pdbe.org/7vpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vpa RCSB], [https://www.ebi.ac.uk/pdbsum/7vpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vpa ProSAT]</span></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]] 2.35Å</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=7vpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vpa OCA], [https://pdbe.org/7vpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vpa RCSB], [https://www.ebi.ac.uk/pdbsum/7vpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vpa ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Polybutylene adipate terephthalate (PBAT) is a biodegradable alternative to polyethylene and can be broadly used in various applications. These polymers can be degraded by hydrolases of terrestrial and aquatic origin. In a previous study, we identified tandem PETase-like hydrolases (Ples) from the marine microbial consortium I1 that were highly expressed when a PBAT blend was supplied as the only carbon source. In this study, the tandem Ples, Ple628 and Ple629, were recombinantly expressed and characterized. Both enzymes are mesophilic and active on a wide range of oligomers. The activities of the Ples differed greatly when model substrates, PBAT-modified polymers or PET nanoparticles were supplied. Ple629 was always more active than Ple628. Crystal structures of Ple628 and Ple629 revealed a structural similarity to other PETases and can be classified as member of the PETases IIa subclass, alpha/beta hydrolase superfamily. Our results show that the predicted functions of Ple628 and Ple629 agree with the bioinformatic predictions, and these enzymes play a significant role in the plastic degradation by the consortium. | |||
Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.,Meyer Cifuentes IE, Wu P, Zhao Y, Liu W, Neumann-Schaal M, Pfaff L, Barys J, Li Z, Gao J, Han X, Bornscheuer UT, Wei R, Ozturk B Front Bioeng Biotechnol. 2022 Jul 21;10:930140. doi: 10.3389/fbioe.2022.930140., eCollection 2022. PMID:35935485<ref>PMID:35935485</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7vpa" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Unclassified Marinobacter]] | |||
[[Category: Basak O]] | [[Category: Basak O]] | ||
[[Category: Gao J]] | [[Category: Gao J]] | ||
Revision as of 20:29, 29 November 2023
Crystal structure of Ple629 from marine microbial consortiumCrystal structure of Ple629 from marine microbial consortium
Structural highlights
Publication Abstract from PubMedPolybutylene adipate terephthalate (PBAT) is a biodegradable alternative to polyethylene and can be broadly used in various applications. These polymers can be degraded by hydrolases of terrestrial and aquatic origin. In a previous study, we identified tandem PETase-like hydrolases (Ples) from the marine microbial consortium I1 that were highly expressed when a PBAT blend was supplied as the only carbon source. In this study, the tandem Ples, Ple628 and Ple629, were recombinantly expressed and characterized. Both enzymes are mesophilic and active on a wide range of oligomers. The activities of the Ples differed greatly when model substrates, PBAT-modified polymers or PET nanoparticles were supplied. Ple629 was always more active than Ple628. Crystal structures of Ple628 and Ple629 revealed a structural similarity to other PETases and can be classified as member of the PETases IIa subclass, alpha/beta hydrolase superfamily. Our results show that the predicted functions of Ple628 and Ple629 agree with the bioinformatic predictions, and these enzymes play a significant role in the plastic degradation by the consortium. Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.,Meyer Cifuentes IE, Wu P, Zhao Y, Liu W, Neumann-Schaal M, Pfaff L, Barys J, Li Z, Gao J, Han X, Bornscheuer UT, Wei R, Ozturk B Front Bioeng Biotechnol. 2022 Jul 21;10:930140. doi: 10.3389/fbioe.2022.930140., eCollection 2022. PMID:35935485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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