6ths
From Proteopedia
(Difference between revisions)
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==High resolution crystal structure of Leaf-branch cutinase S165A variant== | ==High resolution crystal structure of Leaf-branch cutinase S165A variant== | ||
| - | <StructureSection load='6ths' size='340' side='right'caption='[[6ths]]' scene=''> | + | <StructureSection load='6ths' size='340' side='right'caption='[[6ths]], [[Resolution|resolution]] 1.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THS OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6ths]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THS FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene></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=6ths FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ths OCA], [https://pdbe.org/6ths PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ths RCSB], [https://www.ebi.ac.uk/pdbsum/6ths PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ths ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PETH_UNKP PETH_UNKP] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:22194294). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters), with a preference for short-chain substrates (C4 substrate at most) (PubMed:22194294, PubMed:24593046). Cannot hydrolyze olive oil (PubMed:22194294). Is also able to degrade poly(ethylene terephthalate), the most abundant polyester plastic in the world (PubMed:22194294, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:22194294).<ref>PMID:22194294</ref> <ref>PMID:24593046</ref> <ref>PMID:32269349</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Present estimates suggest that of the 359 million tons of plastics produced annually worldwide(1), 150-200 million tons accumulate in landfill or in the natural environment(2). Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging(3). The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties(4). Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse(5). Several PET hydrolase enzymes have been reported, but show limited productivity(6,7). Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme(8,9) from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme(10)) and related improved variants(11-14) that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. | ||
| + | |||
| + | An engineered PET depolymerase to break down and recycle plastic bottles.,Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, Kamionka E, Desrousseaux ML, Texier H, Gavalda S, Cot M, Guemard E, Dalibey M, Nomme J, Cioci G, Barbe S, Chateau M, Andre I, Duquesne S, Marty A Nature. 2020 Apr;580(7802):216-219. doi: 10.1038/s41586-020-2149-4. Epub 2020 Apr, 8. PMID:32269349<ref>PMID:32269349</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ths" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Uncultured bacterium]] | ||
[[Category: Nomme J]] | [[Category: Nomme J]] | ||
Revision as of 13:02, 24 January 2024
High resolution crystal structure of Leaf-branch cutinase S165A variant
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