8ve9

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Current revision (05:55, 19 June 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8ve9 is ON HOLD until Paper Publication
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==IsPETase - ACCCETN mutant - CombiPETase==
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<StructureSection load='8ve9' size='340' side='right'caption='[[8ve9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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Authors: Joho, Y., Royan, S., Newton, S., Caputo, A.T., Ardevol Grau, A., Jackson, C.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ve9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ideonella_sakaiensis Ideonella sakaiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VE9 FirstGlance]. <br>
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Description: IsPETase -ACCCETN mutant -CombiPETase
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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[[Category: Newton, S]]
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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=8ve9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ve9 OCA], [https://pdbe.org/8ve9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ve9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ve9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ve9 ProSAT]</span></td></tr>
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[[Category: Jackson, C]]
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</table>
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[[Category: Ardevol Grau, A]]
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== Function ==
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[[Category: Caputo, A.T]]
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[https://www.uniprot.org/uniprot/PETH_PISS1 PETH_PISS1] Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET (PubMed:26965627). Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product (PubMed:26965627, PubMed:29235460, PubMed:29374183, PubMed:29603535, PubMed:29666242, PubMed:32269349). Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties (PubMed:29666242). In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS) (PubMed:29666242). Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed (PubMed:26965627, PubMed:29374183, PubMed:29603535). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro (PubMed:26965627, PubMed:30502092).<ref>PMID:26965627</ref> <ref>PMID:29235460</ref> <ref>PMID:29374183</ref> <ref>PMID:29603535</ref> <ref>PMID:29666242</ref> <ref>PMID:30502092</ref> <ref>PMID:32269349</ref>
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[[Category: Joho, Y]]
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== References ==
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[[Category: Royan, S]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ideonella sakaiensis]]
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[[Category: Large Structures]]
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[[Category: Ardevol Grau A]]
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[[Category: Caputo AT]]
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[[Category: Jackson C]]
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[[Category: Joho Y]]
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[[Category: Newton S]]
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[[Category: Royan S]]

Current revision

IsPETase - ACCCETN mutant - CombiPETase

PDB ID 8ve9

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