Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?

ABSTRACT: The evolutionary variability of a protein's residues is highly dependent on protein region and function. Solvent-exposed residues, excluding those at interaction interfaces, are more variable than buried residues whereas active site residues are considered to be conserved. The abovementioned rules apply also to α/β-hydrolase fold proteins-one of the oldest and the biggest superfamily of enzymes with buried active sites equipped with tunnels linking the reaction site with the exterior. We selected soluble epoxide hydrolases as representative of this family to conduct the first systematic study on the evolution of tunnels. We hypothesised that tunnels are lined by mostly conserved residues, and are equipped with a number of specific variable residues that are able to respond to evolutionary

SUBMITTER: Bzowka M 

PROVIDER: S-EPMC9140254 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature