9J1E

ESTS1 phthalate ester degrading esterase from Sulfobacillus acidophilus at 1.22A

Summary for 9J1E

• Entry DOI: 10.2210/pdb9j1e/pdb
• Descriptor: Alpha/beta hydrolase fold-3 domain-containing protein, 1,2-ETHANEDIOL, MALONATE ION, ... (5 entities in total)
• Functional Keywords: ests1, phthalate ester degrading esterase, sulfobacillus acidophilus, hydrolase
• Biological source: Sulfobacillus acidophilus DSM 10332
• Total number of polymer chains: 1
• Total formula weight: 34881.55

Authors

Verma, S.,Kumar, P. (deposition date: 2024-08-04, release date: 2024-12-25)

Primary citation

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, 2024

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

Experimental method

X-RAY DIFFRACTION (1.22 Å)