9j1e

ESTS1 phthalate ester degrading esterase from Sulfobacillus acidophilus at 1.22A

spinqualitylabelsall models 9j1e, resolution 1.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9j1e is a 1 chain structure with sequence from Sulfobacillus acidophilus DSM 10332. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.22Å Ligands: ACE, EDO, MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G8TV28_SULAD Publication Abstract from PubMed 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. Mechanistic and structural insights into EstS1 esterase: A potent broad-spectrum phthalate diester degrading enzyme.,Verma S, Choudhary S, Amith Kumar K, Mahto JK, Vamsi K AK, Mishra I, Prakash VB, Sircar D, Tomar S, Kumar Sharma A, Singla J, Kumar P Structure. 2024 Nov 28:S0969-2126(24)00496-9. doi: 10.1016/j.str.2024.11.006. PMID:39642872 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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