4cg3: Difference between revisions

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 <StructureSection load='4cg3' size='340' side='right'caption='[[4cg3]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cg3]] 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=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cg1|4cg1]], [[4cg2|4cg2]]</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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [https://pdbe.org/4cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
-<tr id='activity'><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://pdbe.org/4cg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU]] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). 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 (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). 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>
-Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.
-Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca.,Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714<ref>PMID:24728714</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4cg3" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Thermonospora fusca henssen 1957]]
-[[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]]