7Q04

Crystal structure of TPADO in a substrate-free state

7Q04 の概要

• エントリーDOI: 10.2210/pdb7q04/pdb
• 分子名称: 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)
• 機能のキーワード: terephthalic acid, tpa, oxidoreductase
• 由来する生物種: Comamonas sp.; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 211163.02

構造登録者

Zahn, M.,Kincannon, W.M.,DuBois, J.L.,McGeehan, J.E. (登録日: 2021-10-14, 公開日: 2022-04-06, 最終更新日: 2024-11-13)

主引用文献

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

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: 35312352
DOI: 10.1073/pnas.2121426119

実験手法

X-RAY DIFFRACTION (2.281 Å)