View source for 6qgc


==PETase from Ideonella sakaiensis without ligand==
<StructureSection load='6qgc' size='340' side='right'caption='[[6qgc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qgc]] is a 4 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=6QGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QGC 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]] 2&#8491;</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=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=6qgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qgc OCA], [https://pdbe.org/6qgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qgc RCSB], [https://www.ebi.ac.uk/pdbsum/6qgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qgc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PETH_IDESA PETH_IDESA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The extreme durability of polyethylene terephthalate (PET) debris has rendered it a long-term environmental burden. At the same time, current recycling efforts still lack sustainability. Two recently discovered bacterial enzymes that specifically degrade PET represent a promising solution. First, Ideonella sakaiensis PETase, a structurally well-characterized consensus alpha/beta-hydrolase fold enzyme, converts PET to mono-(2-hydroxyethyl) terephthalate (MHET). MHETase, the second key enzyme, hydrolyzes MHET to the PET educts terephthalate and ethylene glycol. Here, we report the crystal structures of active ligand-free MHETase and MHETase bound to a nonhydrolyzable MHET analog. MHETase, which is reminiscent of feruloyl esterases, possesses a classic alpha/beta-hydrolase domain and a lid domain conferring substrate specificity. In the light of structure-based mapping of the active site, activity assays, mutagenesis studies and a first structure-guided alteration of substrate specificity towards bis-(2-hydroxyethyl) terephthalate (BHET) reported here, we anticipate MHETase to be a valuable resource to further advance enzymatic plastic degradation.

Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate.,Palm GJ, Reisky L, Bottcher D, Muller H, Michels EAP, Walczak MC, Berndt L, Weiss MS, Bornscheuer UT, Weber G Nat Commun. 2019 Apr 12;10(1):1717. doi: 10.1038/s41467-019-09326-3. PMID:30979881<ref>PMID:30979881</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qgc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ideonella sakaiensis]]
[[Category: Large Structures]]
[[Category: Berndt L]]
[[Category: Boettcher D]]
[[Category: Bornscheuer UT]]
[[Category: Michels EAP]]
[[Category: Mueller H]]
[[Category: Palm GJ]]
[[Category: Reisky L]]
[[Category: Walczak C]]
[[Category: Weber G]]
[[Category: Weiss MS]]