7XTU

The structure of TfCut S130A

7XTU の概要

• エントリーDOI: 10.2210/pdb7xtu/pdb
• 分子名称: alpha/beta hydrolase, SULFATE ION, ACETATE ION, ... (7 entities in total)
• 機能のキーワード: pet hydrolase, pbat hydrolase, enzyme engineering, cutinase, hydrolase
• 由来する生物種: Thermobifida fusca (Thermomonospora fusca)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114677.26

構造登録者

Yang, Y.,Jiang, P.C.,Huang, J.-W.,Chen, C.-C.,Guo, R.-T. (登録日: 2022-05-18, 公開日: 2023-03-29, 最終更新日: 2024-10-16)

主引用文献

Yang, Y.,Min, J.,Xue, T.,Jiang, P.,Liu, X.,Peng, R.,Huang, J.W.,Qu, Y.,Li, X.,Ma, N.,Tsai, F.C.,Dai, L.,Zhang, Q.,Liu, Y.,Chen, C.C.,Guo, R.T.
Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases.
Nat Commun, 14:1645-1645, 2023

PubMed Abstract: 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.

PubMed: 36964144
DOI: 10.1038/s41467-023-37374-3

実験手法

X-RAY DIFFRACTION (2.43 Å)