7qjs: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7qjs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJS FirstGlance]. <br>
<table><tr><td colspan='2'>[[7qjs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.429&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=7qjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjs OCA], [https://pdbe.org/7qjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjs RCSB], [https://www.ebi.ac.uk/pdbsum/7qjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjs 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=7qjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjs OCA], [https://pdbe.org/7qjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjs RCSB], [https://www.ebi.ac.uk/pdbsum/7qjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PETH2_THECS PETH2_THECS] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263).<ref>PMID:23592055</ref> <ref>PMID:28671263</ref> [UniProtKB:A0A0K8P6T7]
[https://www.uniprot.org/uniprot/PETH1_THEFY PETH1_THEFY] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:18658138). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:18658138, PubMed:25545638). Also hydrolyzes the triglyceride triolein (PubMed:18658138). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638).<ref>PMID:18658138</ref> <ref>PMID:25545638</ref>  
== References ==
== References ==
<references/>
<references/>

Latest revision as of 12:06, 17 October 2024

Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)

Structural highlights

7qjs is a 2 chain structure with sequence from Thermobifida fusca YX. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.429Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PETH1_THEFY Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:18658138). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:18658138, PubMed:25545638). Also hydrolyzes the triglyceride triolein (PubMed:18658138). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638).[1] [2]

References

  1. ↑ Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J. Identification and characterization of bacterial cutinase. J Biol Chem. 2008 Sep 19;283(38):25854-62. PMID:18658138 doi:10.1074/jbc.M800848200
  2. ↑ Then J, Wei R, Oeser T, Barth M, Belisario-Ferrari MR, Schmidt J, Zimmermann W. Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca. Biotechnol J. 2015 Apr;10(4):592-8. doi: 10.1002/biot.201400620. Epub 2015 Jan, 19. PMID:25545638 doi:http://dx.doi.org/10.1002/biot.201400620

7qjs, resolution 1.43Å

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