Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entrop...
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| Autores principales: | , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
The Royal Society
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/742a9bfe43b248879d57a96a80adc331 |
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