10xn

Crystal structure of a thermophilic esterase from Thermoplasma acidophilum.

spinqualitylabelsall models 10xn, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 10xn is a 2 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HJS7_THEAC Publication Abstract from PubMed Microbial esterases are versatile and stable enzymes with a wide range of biotechnological applications. However, few esterases have been characterized from archaea, an important source of extremophilic enzymes. In this study, we report the biochemical characterization and crystal structure of Ta0887, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum. The protein was successfully cloned, expressed, and purified in Escherichia coli. Light scattering assays revealed that Ta0887 is a monomer in solution. Activity assays using p-nitrophenyl (p-NP) esters confirmed its esterase activity, showing a substrate preference for p-NP hexanoate (C6). Furthermore, the substitution of Ser95 with alanine completely abolished enzymatic activity, thereby confirming its essential role as the nucleophilic residue of the catalytic triad. The enzyme exhibited optimal activity at 65 degrees C and pH 8.0. Notably, Ta0887 displayed high thermal stability, retaining 66% residual activity after incubation at 80 degrees C for 2 h, consistent with its thermal denaturation midpoint temperature of 80.6 degrees C. The crystal structure of Ta0887, resolved at 1.93 A, revealed an alpha/beta-hydrolase core domain consisting of an eight-strand beta-sheet, surrounded by seven alpha-helices, and a cap domain comprising four alpha-helices. Ta0887 features a large substrate-binding pocket at the interface between the two domains that contains the conserved residues Ser95, Asp187, and His215 of the catalytic triad. Further analysis indicates that an efficiently packed hydrophobic core is a key feature for the observed thermostability. The findings from this study provide a basis for the future engineering of Ta0887 with the aim of enhancing its potential for industrial and biotechnological applications. Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.,Delgado-Rey A, Llamas-Garcia ML, Montero-Moran GM, Santos L, Lara-Gonzalez S FEBS Open Bio. 2026 Aug 21:10.1002/2211-5463.70327. doi: 10.1002/2211-5463.70327. PMID:42630012 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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