7qjq

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'''Unreleased structure'''
 
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The entry 7qjq is ON HOLD until Paper Publication
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==Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)==
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<StructureSection load='7qjq' size='340' side='right'caption='[[7qjq]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7qjq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJQ FirstGlance]. <br>
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Description:
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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]] 1.64&#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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7qjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjq OCA], [https://pdbe.org/7qjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjq RCSB], [https://www.ebi.ac.uk/pdbsum/7qjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:23604968, PubMed:24728714, PubMed:31690819, Ref.4). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:15638529, PubMed:23604968, PubMed:24728714, PubMed:25545638, PubMed:31690819, Ref.4). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638, PubMed:31690819, PubMed:32269349, Ref.4). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
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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: Thermobifida fusca]]
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[[Category: Avilan L]]
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[[Category: Beckham GT]]
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[[Category: Gill RS]]
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[[Category: McGeehan JE]]
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[[Category: Zahn M]]

Current revision

Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)

PDB ID 7qjq

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