Transmembrane domain three contributes to the ion conductance pathway of channelrhodopsin-2.

ABSTRACT: Channelrhodopsin-2 (ChR2) is a light-activated nonselective cation channel that is found in the eyespot of the unicellular green alga Chlamydomonas reinhardtii. Despite the wide employment of this protein to control the membrane potential of excitable membranes, the molecular determinants that define the unique ion conductance properties of this protein are not well understood. To elucidate the cation permeability pathway of ion conductance, we performed cysteine scanning mutagenesis of transmembrane domain three followed by labeling with methanethiosulfonate derivatives. An analysis of our experimental results as modeled onto the crystal structure of the C1C2 chimera demonstrate that the ion permeation pathway includes residues on one face of transmembrane domain three at the extracellula

SUBMITTER: Gaiko O 

PROVIDER: S-EPMC3602760 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature