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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Váldodahkkit:	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
Materiálatiipa:	Artigo
Giella:	Inglês
Almmustuhtton:	The Royal Society 2021-12-01
Ráidu:	Open Biology
Fáttát:	serine esterase molecular dynamics enzyme structure protein stability structure–function
Liŋkkat:	https://royalsocietypublishing.org/doi/10.1098/rsob.210182
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