8bra

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'''Unreleased structure'''
 
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The entry 8bra is ON HOLD until Paper Publication
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==Polyester Hydrolase Leipzig 7 (PHL7) bound to terephthalic acid (TPA) and Mg2+==
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<StructureSection load='8bra' size='340' side='right'caption='[[8bra]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8bra]] 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=8BRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UB7:terephthalic+acid'>UB7</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bra OCA], [https://pdbe.org/8bra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bra RCSB], [https://www.ebi.ac.uk/pdbsum/8bra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bra ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 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.
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Authors:
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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<ref>PMID:37019924</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8bra" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Unidentified]]
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[[Category: Richter PK]]
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[[Category: Strater N]]

Revision as of 09:25, 19 April 2023

Polyester Hydrolase Leipzig 7 (PHL7) bound to terephthalic acid (TPA) and Mg2+

PDB ID 8bra

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