Noby_2021_Biorxiv__

Reference

Title : Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation - Noby_2021_Biorxiv__
Author(s) : Noby N , Auhim HS , Winter S , Worthy HL , Embaby AM , Saeed H , Hussein A , Pudney CR , Rizkallah PJ , Wells SA , Jones DD
Ref : Biorxiv , : , 2021
Abstract :

Cold-active esterases hold great potential for undertaking useful biotransformations at low temperatures. 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 alpha/beta 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 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. Comparison of B-factors with the closest related mesophilic and thermophilic esterases suggests the EstN7 cap region is proportionally less flexible. 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 the main drivers of EstN7's cold adaptation rather than changes in dynamics

PubMedSearch : Noby_2021_Biorxiv__
PubMedID:
Gene_locus related to this paper: 9baci-a0a2k9uv39

Related information

Gene_locus 9baci-a0a2k9uv39
Structure 7B4Q

Citations formats

Noby N, Auhim HS, Winter S, Worthy HL, Embaby AM, Saeed H, Hussein A, Pudney CR, Rizkallah PJ, Wells SA, Jones DD (2021)
Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation
Biorxiv :

Noby N, Auhim HS, Winter S, Worthy HL, Embaby AM, Saeed H, Hussein A, Pudney CR, Rizkallah PJ, Wells SA, Jones DD (2021)
Biorxiv :