6qga: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='6qga' size='340' side='right'caption='[[6qga]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6qga' size='340' side='right'caption='[[6qga]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6qga]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6qga]] is a 6 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=6QGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QGA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J1K:4-(2-hydroxyethylcarbamoyl)benzoic+acid'>J1K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J1K:4-(2-hydroxyethylcarbamoyl)benzoic+acid'>J1K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=6qga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qga OCA], [https://pdbe.org/6qga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qga RCSB], [https://www.ebi.ac.uk/pdbsum/6qga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qga 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/MHETH_IDESA MHETH_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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6qga" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Ideonella sakaiensis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Berndt | [[Category: Berndt L]] | ||
[[Category: Boettcher | [[Category: Boettcher D]] | ||
[[Category: Bornscheuer | [[Category: Bornscheuer UT]] | ||
[[Category: Michels | [[Category: Michels EAP]] | ||
[[Category: Mueller | [[Category: Mueller H]] | ||
[[Category: Palm | [[Category: Palm GJ]] | ||
[[Category: Reisky | [[Category: Reisky L]] | ||
[[Category: Walczak | [[Category: Walczak C]] | ||
[[Category: Weber | [[Category: Weber G]] | ||
[[Category: Weiss | [[Category: Weiss MS]] | ||
Latest revision as of 11:59, 24 January 2024
Crystal structure of Ideonella sakaiensis MHETase bound to the non-hydrolyzable ligand MHETA
| ||||||||||||
