Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism

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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Bibliographic Details
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
Format: article
Language:EN
Published: The Royal Society 2021
Subjects:
serine esterase
molecular dynamics
enzyme structure
protein stability
structure–function
Biology (General)
QH301-705.5
Online Access:https://doaj.org/article/742a9bfe43b248879d57a96a80adc331
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https://doaj.org/article/742a9bfe43b248879d57a96a80adc331

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