5xfz
From Proteopedia
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==Crystal structure of a novel PET hydrolase R103G/S131A mutant from Ideonella sakaiensis 201-F6== | ==Crystal structure of a novel PET hydrolase R103G/S131A mutant from Ideonella sakaiensis 201-F6== | ||
| - | <StructureSection load='5xfz' size='340' side='right' caption='[[5xfz]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='5xfz' size='340' side='right'caption='[[5xfz]], [[Resolution|resolution]] 1.55Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5xfz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFZ OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5xfz]] 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=5XFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XFZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id=' | + | <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=5xfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfz OCA], [https://pdbe.org/5xfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xfz RCSB], [https://www.ebi.ac.uk/pdbsum/5xfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfz ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PETH_PISS1 PETH_PISS1] Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET (PubMed:26965627). Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product (PubMed:26965627, PubMed:29235460, PubMed:29374183, PubMed:29603535, PubMed:29666242, PubMed:32269349). Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties (PubMed:29666242). In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS) (PubMed:29666242). Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed (PubMed:26965627, PubMed:29374183, PubMed:29603535). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro (PubMed:26965627, PubMed:30502092).<ref>PMID:26965627</ref> <ref>PMID:29235460</ref> <ref>PMID:29374183</ref> <ref>PMID:29603535</ref> <ref>PMID:29666242</ref> <ref>PMID:30502092</ref> <ref>PMID:32269349</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated. | ||
| + | |||
| + | Structural insight into catalytic mechanism of PET hydrolase.,Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT Nat Commun. 2017 Dec 13;8(1):2106. doi: 10.1038/s41467-017-02255-z. PMID:29235460<ref>PMID:29235460</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5xfz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Ideonella sakaiensis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chen CC]] |
| - | [[Category: | + | [[Category: Guo RT]] |
| - | [[Category: | + | [[Category: Han X]] |
| - | [[Category: | + | [[Category: Liu WD]] |
| - | [[Category: | + | [[Category: Zheng YY]] |
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Current revision
Crystal structure of a novel PET hydrolase R103G/S131A mutant from Ideonella sakaiensis 201-F6
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Categories: Ideonella sakaiensis | Large Structures | Chen CC | Guo RT | Han X | Liu WD | Zheng YY
