6aid
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structural insights into the unique polylactate degrading mechanism of Thermobifida alba cutinase== | |
| + | <StructureSection load='6aid' size='340' side='right'caption='[[6aid]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6aid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_alba Thermobifida alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AID 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]] 1.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9YL:ethyl+(2R)-2-oxidanylpropanoate'>9YL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6aid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aid OCA], [https://pdbe.org/6aid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aid RCSB], [https://www.ebi.ac.uk/pdbsum/6aid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aid ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PETH2_THEAE PETH2_THEAE] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA) (PubMed:20393707, PubMed:22183084).[UniProtKB:D4Q9N1]<ref>PMID:20393707</ref> <ref>PMID:22183084</ref> <ref>PMID:25910960</ref> <ref>PMID:33387709</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cutinases are enzymes known to degrade polyester-type plastics. Est119, a plastic-degrading type of cutinase from Thermobifida alba AHK119 (herein called Ta_cut), shows a broad substrate specificity toward polyesters, and can degrade substrates including polylactic acid (PLA). However, the PLA-degrading mechanism of cutinases is still poorly understood. Here, we report the structure complexes of cutinase with ethyl lactate (EL), the constitutional unit. From this complex structure, the electron density maps clearly showed one lactate (LAC) and one EL occupying different positions in the active site cleft. The binding mode of EL is assumed to show a figure prior to reaction and LAC is an after-reaction product. These complex structures demonstrate the role of active site residues in the esterase reaction and substrate recognition. The complex structures were compared with other documented complex structures of cutinases and with the structure of PETase from Ideonella sakaiensis. The amino acid residues involved in substrate interaction are highly conserved among these enzymes. Thus, mapping the precise interactions in the Ta_cut and EL complex will pave the way for understanding the plastic-degrading mechanism of cutinases and suggest ways of creating more potent enzymes by structural protein engineering. This article is protected by copyright. All rights reserved. | ||
| - | + | Structural insights into the unique polylactate-degrading mechanism of Thermobifida alba cutinase.,Kitadokoro K, Mizuki K, Matsui S, Osokoshi R, Uschara T, Kawai F, Kamitani S FEBS J. 2019 Feb 14. doi: 10.1111/febs.14781. PMID:30761732<ref>PMID:30761732</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6aid" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermobifida alba]] | ||
| + | [[Category: Kakara M]] | ||
| + | [[Category: Kamitani S]] | ||
| + | [[Category: Kawai F]] | ||
| + | [[Category: Kitadokoro K]] | ||
| + | [[Category: Matsui S]] | ||
| + | [[Category: Osokoshi R]] | ||
| + | [[Category: Thumarat U]] | ||
Current revision
Structural insights into the unique polylactate degrading mechanism of Thermobifida alba cutinase
| |||||||||||
