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:English
Published: The Royal Society 2021-12-01
Series:Open Biology
Subjects:
serine esterase
molecular dynamics
enzyme structure
protein stability
structure–function
Online Access:https://royalsocietypublishing.org/doi/10.1098/rsob.210182

Internet

https://royalsocietypublishing.org/doi/10.1098/rsob.210182

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