View source for 7q06


==Crystal structure of TPADO in complex with 2-OH-TPA==
<StructureSection load='7q06' size='340' side='right'caption='[[7q06]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7q06]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_sp. Comamonas sp.] and [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q06 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8IB:2-oxidanylterephthalic+acid'>8IB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=7q06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q06 OCA], [https://pdbe.org/7q06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q06 RCSB], [https://www.ebi.ac.uk/pdbsum/7q06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q06 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPDB1_COMSP TPDB1_COMSP] Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.<ref>PMID:16517628</ref> <ref>PMID:18776687</ref> <ref>PMID:7961417</ref> 
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== Publication Abstract from PubMed ==
SignificanceMore than 400 million tons of plastic waste is produced each year, the overwhelming majority of which ends up in landfills. Bioconversion strategies aimed at plastics have emerged as important components of enabling a circular economy for synthetic plastics, especially those that exhibit chemically similar linkages to those found in nature, such as polyesters. The enzyme system described in this work is essential for mineralization of the xenobiotic components of poly(ethylene terephthalate) (PET) in the biosphere. Our description of its structure and substrate preferences lays the groundwork for in vivo or ex vivo engineering of this system for PET upcycling.

Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.,Kincannon WM, Zahn M, Clare R, Lusty Beech J, Romberg A, Larson J, Bothner B, Beckham GT, McGeehan JE, DuBois JL Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2121426119. doi: , 10.1073/pnas.2121426119. Epub 2022 Mar 21. PMID:35312352<ref>PMID:35312352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q06" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Comamonas sp]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: DuBois JL]]
[[Category: Kincannon WM]]
[[Category: McGeehan JE]]
[[Category: Zahn M]]