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8jmp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a leaf-branch compost cutinase, ICCG in complex with 1,4-butanediol terephthalate== | |
| + | <StructureSection load='8jmp' size='340' side='right'caption='[[8jmp]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8jmp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified_prokaryotic_organism Unidentified prokaryotic organism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JMP FirstGlance]. <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]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EMX:4-[4-(4-carboxyphenyl)carbonyloxybutoxycarbonyl]benzoic+acid'>EMX</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=8jmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jmp OCA], [https://pdbe.org/8jmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jmp RCSB], [https://www.ebi.ac.uk/pdbsum/8jmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jmp ProSAT]</span></td></tr> | ||
| + | </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 == | ||
| + | Poly(butylene adipate-co-terephthalate) (PBAT) is among the most widely applied synthetic polyesters that are utilized in the packaging and agricultural industries, but the accumulation of PBAT wastes has posed a great burden to ecosystems. Using renewable enzymes to decompose PBAT is an eco-friendly solution to tackle this problem. Recently, we demonstrated that cutinase is the most effective PBAT-degrading enzyme and that an engineered cutinase termed TfCut-DM could completely decompose PBAT film to terephthalate (TPA). Here, we report crystal structures of a variant of leaf compost cutinase in complex with soluble fragments of PBAT, including BTa and TaBTa. In the TaBTa complex, one TPA moiety was located at a polymer-binding site distal to the catalytic center that has never been experimentally validated. Intriguingly, the composition of the distal TPA-binding site shows higher diversity relative to the one proximal to the catalytic center in various cutinases. We thus modified the distal TPA-binding site of TfCut-DM and obtained variants that exhibit higher activity. Notably, the time needed to completely degrade the PBAT film to TPA was shortened to within 24 h by TfCut-DM Q132Y (5813 mol per mol protein). Taken together, the structural information regarding the substrate-binding behavior of PBAT-degrading enzymes could be useful guidance for direct enzyme engineering. | ||
| - | + | Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme.,Yang Y, Cheng S, Zheng Y, Xue T, Huang JW, Zhang L, Yang Y, Guo RT, Chen CC J Hazard Mater. 2023 Nov 10;464:132965. doi: 10.1016/j.jhazmat.2023.132965. PMID:37979420<ref>PMID:37979420</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Chen | + | <div class="pdbe-citations 8jmp" style="background-color:#fffaf0;"></div> |
| - | [[Category: Cheng | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Unidentified prokaryotic organism]] | ||
| + | [[Category: Chen C-C]] | ||
| + | [[Category: Cheng S]] | ||
| + | [[Category: Guo R-T]] | ||
| + | [[Category: Xue T]] | ||
| + | [[Category: Yang Y]] | ||
| + | [[Category: Zheng Y]] | ||
Current revision
Structure of a leaf-branch compost cutinase, ICCG in complex with 1,4-butanediol terephthalate
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