8brb: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8brb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRB FirstGlance]. <br> | <table><tr><td colspan='2'>[[8brb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=UB7:terephthalic+acid'>UB7</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]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=UB7:terephthalic+acid'>UB7</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=8brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brb OCA], [https://pdbe.org/8brb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brb RCSB], [https://www.ebi.ac.uk/pdbsum/8brb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brb 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=8brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brb OCA], [https://pdbe.org/8brb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brb RCSB], [https://www.ebi.ac.uk/pdbsum/8brb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 16:40, 1 February 2024
Polyester Hydrolase Leipzig 7 (PHL7) bound to terephthalic acid (TPA)Polyester Hydrolase Leipzig 7 (PHL7) bound to terephthalic acid (TPA)
Structural highlights
Publication Abstract from PubMedThe recently discovered metagenomic-derived polyester hydrolase PHL7 is able to efficiently degrade amorphous polyethylene terephthalate (PET) in post-consumer plastic waste. We present the cocrystal structure of this hydrolase with its hydrolysis product terephthalic acid and elucidate the influence of 17 single mutations on the PET-hydrolytic activity and thermal stability of PHL7. The substrate-binding mode of terephthalic acid is similar to that of the thermophilic polyester hydrolase LCC and deviates from the mesophilic IsPETase. The subsite I modifications L93F and Q95Y, derived from LCC, increased the thermal stability, while exchange of H185S, derived from IsPETase, reduced the stability of PHL7. The subsite II residue H130 is suggested to represent an adaptation for high thermal stability, whereas L210 emerged as the main contributor to the observed high PET-hydrolytic activity. Variant L210T showed significantly higher activity, achieving a degradation rate of 20 microm h(-1) with amorphous PET films. Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product.,Richter PK, Blazquez-Sanchez P, Zhao Z, Engelberger F, Wiebeler C, Kunze G, Frank R, Krinke D, Frezzotti E, Lihanova Y, Falkenstein P, Matysik J, Zimmermann W, Strater N, Sonnendecker C Nat Commun. 2023 Apr 5;14(1):1905. doi: 10.1038/s41467-023-37415-x. PMID:37019924[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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