9J5C

ESTS1 phthalate ester degrading esterase from Sulfobacillus acidophilus in complex with diethylhexyl phthalate

9J5C の概要

• エントリーDOI: 10.2210/pdb9j5c/pdb
• 分子名称: Alpha/beta hydrolase fold-3 domain-containing protein, ~{O}1-[(2~{R})-2-ethylhexyl] ~{O}2-[(2~{S})-2-ethylhexyl] benzene-1,2-dicarboxylate (3 entities in total)
• 機能のキーワード: ests1, phthalate ester degrading esterase, diethylhexyl phthalate, hydrolase
• 由来する生物種: Sulfobacillus acidophilus DSM 10332
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34957.95

構造登録者

Verma, S.,Kumar, P. (登録日: 2024-08-11, 公開日: 2024-12-25, 最終更新日: 2025-02-19)

主引用文献

Verma, S.,Choudhary, S.,Amith Kumar, K.,Mahto, J.K.,Vamsi K, A.K.,Mishra, I.,Prakash, V.B.,Sircar, D.,Tomar, S.,Kumar Sharma, A.,Singla, J.,Kumar, P.
Mechanistic and structural insights into EstS1 esterase: A potent broad-spectrum phthalate diester degrading enzyme.
Structure, 33:247-261.e3, 2025

PubMed Abstract: Phthalate diesters are important pollutants and act as endocrine disruptors. While certain bacterial esterases have been identified for phthalate diesters degradation to monoesters, their structural and mechanistic characteristics remain largely unexplored. Here, we highlight the potential of the thermostable and pH-tolerant EstS1 esterase from Sulfobacillus acidophilus DSM10332 to degrade high molecular weight bis(2-ethylhexyl) phthalate (DEHP) by combining biophysical and biochemical approaches along with high-resolution EstS1 crystal structures of the apo form and with bound substrates, products, and their analogs to elucidate its mechanism. The catalytic tunnel mediates entry and exit of the substrate and product, respectively. The centralized Ser-His-Asp triad performs catalysis by a bi-bi ping-pong mechanism, forming a tetrahedral intermediate. Mutagenesis analysis showed that the Met207Ala mutation abolished DEHP binding at the active site, confirming its essential role in supporting catalysis. These findings underscore EstS1 as a promising tool for advancing technologies aimed at phthalate diesters biodegradation.

PubMed: 39642872
DOI: 10.1016/j.str.2024.11.006

実験手法

X-RAY DIFFRACTION (2.7 Å)