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5yfe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5yfe is ON HOLD Authors: Bao, R., He, L.H., Liu, B. Description: Enzymatic and structural characterization of the poly (ethylene terephthalate) hyd...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis== | |
| + | <StructureSection load='5yfe' size='340' side='right'caption='[[5yfe]], [[Resolution|resolution]] 1.39Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5yfe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ideonella_sakaiensis Ideonella sakaiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YFE 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]] 1.39Å</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=SO4:SULFATE+ION'>SO4</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=5yfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yfe OCA], [https://pdbe.org/5yfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yfe RCSB], [https://www.ebi.ac.uk/pdbsum/5yfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yfe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PETH_IDESA PETH_IDESA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis. | ||
| - | + | Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis.,Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R Chembiochem. 2018 Mar 30. doi: 10.1002/cbic.201800097. PMID:29603535<ref>PMID:29603535</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bao | + | <div class="pdbe-citations 5yfe" style="background-color:#fffaf0;"></div> |
| - | [[Category: He | + | == References == |
| - | [[Category: Liu | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ideonella sakaiensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bao R]] | ||
| + | [[Category: He LH]] | ||
| + | [[Category: Liu B]] | ||
Current revision
Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis
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