Molecular mechanism of substrate selectivity of the arginine-agmatine Antiporter AdiC.

ABSTRACT: The arginine-agmatine antiporter (AdiC) is a component of an acid resistance system developed by enteric bacteria to resist gastric acidity. In order to avoid neutral proton antiport, the monovalent form of arginine, about as abundant as its divalent form under acidic conditions, should be selectively bound by AdiC for transport into the cytosol. In this study, we shed light on the mechanism through which AdiC distinguishes Arg⁺ from Arg²⁺ of arginine by investigating the binding of both forms in addition to that of divalent agmatine, using a combination of molecular dynamics simulations with molecular and quantum mechanics calculations. We show that AdiC indeed preferentially binds Arg⁺. The weaker binding of divalent compounds results mostly from their gr

SUBMITTER: Krammer EM 

PROVIDER: S-EPMC6199258 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature