Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy

Channelrhodopsin is a cation channel with the unique property of being activated by light. To address structural changes of the open state of the channel, two variants, which contain either 1 or 2 wild-type cysteines, were derivatised with nitroxide spin label and subjected to electron paramagnetic resonance spectroscopy. Both variants contained the C128T mutation to trap the long-lived P-3(520) state by illumination. Comparison of spin-spin distances in the dark state and after illumination reflect conformational changes in the conductive P-3(520) state involving helices B and F. Spin distance measurements reveal that channelrhodopsin forms a dimer even in the absence of intermolecular N-terminal cysteines. Structured summary of protein interactions: ChR2 and ChR2bind by electron resonance (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.