Electrostatic Preorganization in Three Distinct Heterogeneous Proteasome β-Subunits.

ABSTRACT: The origin of the enzyme's powerful role in accelerating chemical reactions is one of the most critical and still widely discussed questions. It is already accepted that enzymes impose an electrostatic field onto their substrates by adopting complex three-dimensional structures; therefore, the preorganization of electric fields inside protein active sites has been proposed as a crucial contributor to catalytic mechanisms and rate constant enhancement. In this work, we focus on three catalytically active β-subunits of 20S proteasomes with low sequence identity (∼30%) whose active sites, although situated in an electrostatically miscellaneous environment, catalyze the same chemical reaction with similar catalytic efficiency. Our in silico experiments reproduce the experimentally observed equ

SUBMITTER: Ferrer S 

PROVIDER: S-EPMC11494509 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature