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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Main Authors: | Nehad Noby, Husam Sabah Auhim, Samuel Winter, Harley L. Worthy, Amira M. Embaby, Hesham Saeed, Ahmed Hussein, Christopher R. Pudney, Pierre J. Rizkallah, Stephen A. Wells, D. Dafydd Jones |
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Format: | article |
Language: | EN |
Published: |
The Royal Society
2021
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Subjects: | |
Online Access: | https://doaj.org/article/742a9bfe43b248879d57a96a80adc331 |
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