8jmo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of a leaf-branch compost cutinase, ICCG in complex with 4-((4-Hydroxybutoxy)carbonyl)benzoic acid== | |||
<StructureSection load='8jmo' size='340' side='right'caption='[[8jmo]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8jmo]] 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=8JMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JMO 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]] 1.95Å</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=E7J:4-(4-oxidanylbutoxycarbonyl)benzoic+acid'>E7J</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=8jmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jmo OCA], [https://pdbe.org/8jmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jmo RCSB], [https://www.ebi.ac.uk/pdbsum/8jmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jmo 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> | ||
<div class="pdbe-citations 8jmo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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]] | |||