Collaboration between IQFR scientists, CBM Severo Ochoa center and the Vigo and A Coruña Universities, together with Galchimia company, reveals unprecedent characteristics in a thermophile esterase, obtained from a hot spring

Esterases and lipases count with keen industrial interest due to its capacity to accept a wide range of non-natural substrates and its stability in organic solvents, and, in the case of extremophile organisms, its ability to tolerate extreme temperatures and pH. In this work, published in the Computational and Structural Biotechnology Journal, a novel esterase, EstD11, has been biochemically and structurally characterized. The tridimensional structure of EstD11 and the inactive mutant has been determined together with 8 crystallographic complexes with different substrates and products of the esterase reaction revealing the molecular basis underlying enzyme reactivity and specificity. Interestingly, a unique methionine zipper has been identified lining the active site and cap domains that may be responsible for the thermostability and catalytic promiscuity of the protein. Furthermore, the success of high-temperature crystallization experiments has been key in obtaining singular information on cap dynamics.


Vega Miguel-Ruano, Ivanna Rivera, Jelena Rajkovic, Kamila Knapik, Ana Torrado, José Manuel Otero, Elisa Beneventi, Manuel Becerra, Mercedes Sánchez, Aurelio Hidalgo, José Berenguer, María Isabel Gonzalez-Siso, Jacobo Cruces, María Luisa Rúa, Juan A. Hermoso, Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family, Computational and Structural Biotechnology Journal, 2021, ISSN 2001-0370,