6eqe: Difference between revisions

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 ==High resolution crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis==
-<StructureSection load='6eqe' size='340' side='right' caption='[[6eqe]], [[Resolution|resolution]] 0.92&Aring;' scene=''>
+<StructureSection load='6eqe' size='340' side='right'caption='[[6eqe]], [[Resolution|resolution]] 0.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6eqe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Idesa Idesa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EQE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6eqe]] 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=6EQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EQE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 0.92&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6eqd|6eqd]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ISF6_4831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1547922 IDESA])</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=6eqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqe OCA], [https://pdbe.org/6eqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eqe RCSB], [https://www.ebi.ac.uk/pdbsum/6eqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqe ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(ethylene_terephthalate)_hydrolase Poly(ethylene terephthalate) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.101 3.1.1.101] </span></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=6eqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqe OCA], [http://pdbe.org/6eqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqe RCSB], [http://www.ebi.ac.uk/pdbsum/6eqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqe ProSAT]</span></td></tr>
 </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 ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Idesa]]
+[[Category: Ideonella sakaiensis]]
-[[Category: Allen, M D]]
+[[Category: Large Structures]]
-[[Category: Austin, H P]]
+[[Category: Allen MD]]
-[[Category: Beckham, G T]]
+[[Category: Austin HP]]
-[[Category: Johnson, C W]]
+[[Category: Beckham GT]]
-[[Category: McGeehan, J E]]
+[[Category: Johnson CW]]
-[[Category: A/b hydrolase]]
+[[Category: McGeehan JE]]
-[[Category: Hydrolase]]
-[[Category: Pet degradation]]
-[[Category: Petase]]