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==Crystal structure of Leaf-branch compost bacterial cutinase homolog==
==Crystal structure of Leaf-branch compost bacterial cutinase homolog==
<StructureSection load='4eb0' size='340' side='right' caption='[[4eb0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4eb0' size='340' side='right'caption='[[4eb0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eb0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacterial_sp. Bacterial sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EB0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eb0]] 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=4EB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EB0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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=4eb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eb0 OCA], [http://pdbe.org/4eb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eb0 RCSB], [http://www.ebi.ac.uk/pdbsum/4eb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eb0 ProSAT]</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=4eb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eb0 OCA], [https://pdbe.org/4eb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eb0 RCSB], [https://www.ebi.ac.uk/pdbsum/4eb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eb0 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>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterial sp]]
[[Category: Large Structures]]
[[Category: Cutinase]]
[[Category: Uncultured bacterium]]
[[Category: Eiko, K]]
[[Category: Eiko K]]
[[Category: Kanaya, S]]
[[Category: Kanaya S]]
[[Category: Koga, Y]]
[[Category: Koga Y]]
[[Category: Sulaiman, S]]
[[Category: Sulaiman S]]
[[Category: You, D J]]
[[Category: You DJ]]
[[Category: Cutinase homolog]]
[[Category: Hydrolase]]
[[Category: Metagenome]]
[[Category: Pet degradation]]
[[Category: Serine esterase]]

Latest revision as of 16:47, 8 November 2023

Crystal structure of Leaf-branch compost bacterial cutinase homologCrystal structure of Leaf-branch compost bacterial cutinase homolog

Structural highlights

4eb0 is a 1 chain structure with sequence from Uncultured bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

References

  1. ↑ Sulaiman S, Yamato S, Kanaya E, Kim JJ, Koga Y, Takano K, Kanaya S. Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach. Appl Environ Microbiol. 2012 Mar;78(5):1556-62. doi: 10.1128/AEM.06725-11. Epub, 2011 Dec 22. PMID:22194294 doi:http://dx.doi.org/10.1128/AEM.06725-11
  2. ↑ Sulaiman S, You DJ, Kanaya E, Koga Y, Kanaya S. Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase. Biochemistry. 2014 Mar 25;53(11):1858-69. doi: 10.1021/bi401561p. Epub 2014 Mar, 13. PMID:24593046 doi:http://dx.doi.org/10.1021/bi401561p
  3. ↑ 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. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020 Apr;580(7802):216-219. doi: 10.1038/s41586-020-2149-4. Epub 2020 Apr, 8. PMID:32269349 doi:http://dx.doi.org/10.1038/s41586-020-2149-4

4eb0, resolution 1.50Å

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