Structure and mechanisms of sodium-pumping KR2 rhodopsin

Kirill Kovalev, Vitaly Polovinkin, Ivan Gushchin, Alexey Alekseev, Vitaly Shevchenko, Valentin Borshchevskiy, Roman Astashkin, Taras Balandin, Dmitry Bratanov, S. Vaganova,

Science Advances · 2019 · 95 citations · 46 references

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Abstract

) light-driven pump at physiological pH in its pentameric form. We also present 13 atomic structures and functional data on the KR2 and its mutants, including potassium pumps, which show that oligomerization of the microbial rhodopsin is obligatory for its biological function. The studies reveal the structure of KR2 at nonphysiological low pH where it acts as a proton pump. The structure provides new insights into the mechanisms of microbial rhodopsins and opens the way to a rational design of novel cation pumps for optogenetics.

References

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