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6qgb
From Proteopedia
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<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=6qgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qgb OCA], [http://pdbe.org/6qgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qgb RCSB], [http://www.ebi.ac.uk/pdbsum/6qgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qgb ProSAT]</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=6qgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qgb OCA], [http://pdbe.org/6qgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qgb RCSB], [http://www.ebi.ac.uk/pdbsum/6qgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qgb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6qgb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Ideonella sakaiensis MHETase bound to benzoic acid
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