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

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

SUBMITTER: Noby N 

PROVIDER: S-EPMC8633780 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature