View source for 7xts


==The apo structure of the engineered TfCut S130A==
<StructureSection load='7xts' size='340' side='right'caption='[[7xts]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xts]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTS 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]] 2.21&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7xts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xts OCA], [https://pdbe.org/7xts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xts RCSB], [https://www.ebi.ac.uk/pdbsum/7xts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xts ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Poly(butylene adipate-co-terephthalate) (PBAT), a polyester made of terephthalic acid (TPA), 1,4-butanediol, and adipic acid, is extensively utilized in plastic production and has accumulated globally as environmental waste. Biodegradation is an attractive strategy to manage PBAT, but an effective PBAT-degrading enzyme is required. Here, we demonstrate that cutinases are highly potent enzymes that can completely decompose PBAT films in 48 h. We further show that the engineered cutinases, by applying a double mutation strategy to render a more flexible substrate-binding pocket exhibit higher decomposition rates. Notably, these variants produce TPA as a major end-product, which is beneficial feature for the future recycling economy. The crystal structures of wild type and double mutation of a cutinase from Thermobifida fusca in complex with a substrate analogue are also solved, elucidating their substrate-binding modes. These structural and biochemical analyses enable us to propose the mechanism of cutinase-mediated PBAT degradation.

Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases.,Yang Y, Min J, Xue T, Jiang P, Liu X, Peng R, Huang JW, Qu Y, Li X, Ma N, Tsai FC, Dai L, Zhang Q, Liu Y, Chen CC, Guo RT Nat Commun. 2023 Mar 24;14(1):1645. doi: 10.1038/s41467-023-37374-3. PMID:36964144<ref>PMID:36964144</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xts" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermobifida fusca]]
[[Category: Chen C-C]]
[[Category: Guo R-T]]
[[Category: Huang J-W]]
[[Category: Jiang PC]]
[[Category: Yang Y]]