Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers.

ABSTRACT: Fluoride ion channels of the Fluc family selectively export F^- ions to rescue unicellular organisms from acute F^- toxicity. Crystal structures of bacterial Fluc channels in complex with synthetic monobodies, fibronectin-derived soluble β-sandwich fold proteins, show 2-fold symmetric homodimers with an antiparallel transmembrane topology. Monobodies also block Fluc F^- current via a pore blocking mechanism. However, little is known about the energetic contributions of individual monobody residues to the affinity of the monobody-channel complex or whether the structural paratope corresponds to functional reality. This study seeks to structurally identify and compare residues interacting with Fluc between two highly similar monobodies and subjects them to mutag

SUBMITTER: Turman DL 

PROVIDER: S-EPMC6215451 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature