Mutations conferring SO₄^2- pumping ability on the cyanobacterial anion pump rhodopsin and the resultant unique features of the mutant.

ABSTRACT: Membrane transport proteins can be divided into two types: those that bind substrates in a resting state and those that do not. In this study, we demonstrate that these types can be converted by mutations through a study of two cyanobacterial anion-pumping rhodopsins, Mastigocladopsis repens halorhodopsin (MrHR) and Synechocystis halorhodopsin (SyHR). Anion pump rhodopsins, including MrHR and SyHR, initially bind substrate anions to the protein center and transport them upon illumination. MrHR transports only smaller halide ions, Cl^- and Br^-, but SyHR also transports SO₄^2-, despite the close sequence similarity to MrHR. We sought a determinant that could confer SO₄^2- pumping ability on MrHR and found that the removal of a ne

SUBMITTER: Doi Y 

PROVIDER: S-EPMC9525653 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature