7qjs: Difference between revisions

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'''Unreleased structure'''


The entry 7qjs is ON HOLD  until Paper Publication
==Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)==
 
<StructureSection load='7qjs' size='340' side='right'caption='[[7qjs]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
Authors:  
== 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>
Description:  
</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>
[[Category: Unreleased Structures]]
<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>
== 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]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermobifida fusca YX]]
[[Category: Beckham GT]]
[[Category: McGeehan JE]]
[[Category: Shakespeare TJ]]
[[Category: Zahn M]]

Revision as of 11:47, 28 December 2022

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.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [UniProtKB:A0A0K8P6T7]

References

  1. Herrero Acero E, Ribitsch D, Dellacher A, Zitzenbacher S, Marold A, Steinkellner G, Gruber K, Schwab H, Guebitz GM. Surface engineering of a cutinase from Thermobifida cellulosilytica for improved polyester hydrolysis. Biotechnol Bioeng. 2013 Oct;110(10):2581-90. doi: 10.1002/bit.24930. Epub 2013 , Apr 29. PMID:23592055 doi:http://dx.doi.org/10.1002/bit.24930
  2. Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM. Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica. Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263 doi:http://dx.doi.org/10.1002/bit.26372

7qjs, resolution 1.43Å

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