7Q04
Crystal structure of TPADO in a substrate-free state
Summary for 7Q04
| Entry DOI | 10.2210/pdb7q04/pdb |
| Descriptor | Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1, Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2, Lysozyme, ... (6 entities in total) |
| Functional Keywords | terephthalic acid, tpa, oxidoreductase |
| Biological source | Comamonas sp. More |
| Total number of polymer chains | 7 |
| Total formula weight | 211163.02 |
| Authors | Zahn, M.,Kincannon, W.M.,DuBois, J.L.,McGeehan, J.E. (deposition date: 2021-10-14, release date: 2022-04-06, Last modification date: 2024-11-13) |
| Primary citation | Kincannon, W.M.,Zahn, M.,Clare, R.,Lusty Beech, J.,Romberg, A.,Larson, J.,Bothner, B.,Beckham, G.T.,McGeehan, J.E.,DuBois, J.L. Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism. Proc.Natl.Acad.Sci.USA, 119:e2121426119-e2121426119, 2022 Cited by PubMed Abstract: 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. PubMed: 35312352DOI: 10.1073/pnas.2121426119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.281 Å) |
Structure validation
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