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

Noby, Nehad, Auhim, Husam Sabah, Winter, Samuel, Worthy, Harley L., Embaby, Amira M., Saeed, Hesham, Hussein, Ahmed, Pudney, Christopher R., Rizkallah, Pierre J. ORCID: https://orcid.org/0000-0002-9290-0369, Wells, Stephen A. and Jones, D. Dafydd ORCID: https://orcid.org/0000-0001-7709-3995 2021. Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism. Open Biology 11 (12) , 210182. 10.1098/rsob.210182

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Abstract

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 entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical content providing greater access to the active site through more than one substrate access tunnel. However, dynamics do not appear to play a major role in cold adaption. Molecular dynamics at different temperatures, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are important for of EstN7's cold adaptation rather than changes in dynamics.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine Biosciences Advanced Research Computing @ Cardiff (ARCCA)
Additional Information:	Published under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/
Publisher:	The Royal Society
ISSN:	2046-2441
Date of First Compliant Deposit:	11 January 2022
Date of Acceptance:	2 October 2021
Last Modified:	17 May 2023 00:50
URI:	https://orca.cardiff.ac.uk/id/eprint/146533

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