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==Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca==
==Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca==
<StructureSection load='4cg2' size='340' side='right' caption='[[4cg2]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
<StructureSection load='4cg2' size='340' side='right'caption='[[4cg2]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cg2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cg2]] is a 1 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=4CG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG2 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.437&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cg1|4cg1]], [[4cg3|4cg3]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </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=4cg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg2 OCA], [https://pdbe.org/4cg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg2 ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg2 PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4cg2" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cutinase 3D structures|Cutinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cutinase]]
[[Category: Large Structures]]
[[Category: Foellner, C.]]
[[Category: Thermobifida fusca]]
[[Category: Oeser, T.]]
[[Category: Foellner C]]
[[Category: Roth, C.]]
[[Category: Oeser T]]
[[Category: Straeter, N.]]
[[Category: Roth C]]
[[Category: Then, J.]]
[[Category: Straeter N]]
[[Category: Wei, R.]]
[[Category: Then J]]
[[Category: Zimmermann, W.]]
[[Category: Wei R]]
[[Category: Alpha beta fold]]
[[Category: Zimmermann W]]
[[Category: Hydrolase]]
[[Category: Pet degradation]]

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