Hydrogen-bonding network at the cytoplasmic region of a light-driven sodium pump rhodopsin KR2

Biochimica Et Biophysica Acta. Bioenergetics
Sahoko TomidaHideki Kandori

Abstract

Light-driven sodium-pumping rhodopsins are able to actively transport sodium ions. Structure/function studies of Krokinobacter eikastus rhodopsin 2 (KR2) identified N61 and G263 at the cytoplasmic surface constituting the "Ion-selectivity filter" for sodium ions, while retinal Schiff base acts as the light "Switch and Gate" for transport of sodium ions. Q123 is located between the two regions, and plays an important role for the pump function, which was implicated by functional, spectroscopic, X-ray crystallographic and computational studies. According to the atomic structure of KR2, Q123 is involved in the hydrogen-bonding network at the cytoplasmic region, together with S64, protein-bound waters, and peptide carbonyl of K255 bound to the chromophore. To gain the detailed structural information around Q123, here we compared light-induced difference Fourier-transform infrared (FTIR) spectra at 77 K between the wild-type (WT) and mutant proteins of KR2, such as Q123A, Q123V, and S64A. The obtained spectra were very similar between WT and these mutants, whereas the observed mutation effects enabled us to identify vibrations of the hydrogen-bonding network at the Q123 and S64 region. This is unique for KR2, not for the correspondi...Continue Reading

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Citations

Jul 10, 2021·The Journal of Chemical Physics·Mantu SantraSuman Chakrabarty
Mar 28, 2019·Journal of Chemical Theory and Computation·Laura Pedraza-GonzálezMassimo Olivucci
Aug 20, 2021·Journal of Photochemistry and Photobiology. B, Biology·Shin-Gyu ChoKwang-Hwan Jung

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