Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design

Authors

Sykora, J., Brezovsky, J., Koudelakova, T., Lahoda, M., Fortova, A., Chernovets, T., Chaloupkova, R., Stepankova, V., Prokop, Z., Kuta Smatanova, I., Hof, M., Damborsky, J.

Source

NATURE CHEMICAL BIOLOGY 10: 428-430 (2014)

Abstract

We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.

Full text •  Supplement

Citation

Sykora, J., Brezovsky, J., Koudelakova, T., Lahoda, M., Fortova, A., Chernovets, T., Chaloupkova, R., Stepankova, V., Prokop, Z., Kuta Smatanova, I., Hof, M., Damborsky, J., 2014: Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design. Nature Chemical Biology 10: 428-430.

Stas to Present at Beilstein Symposium 2023
Ihor Received EMBO Grant
Press Release – Article Published in Chem Catalysis
Seminar IBIS in LL
Veronika and Honza – Winners of Student Scientific Conference
Former Ph.D. Student in LL Published in Nature Neuroscience
Martin to Present at ELI User Workshop 2022

More news