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Crystal structure of a light-driven sodium pump

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Bamann,  Christian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Gushchin, I., Shevchenko, V., Polovinkin, V., Kovalev, K., Alekseev, A., Round, E., et al. (2015). Crystal structure of a light-driven sodium pump. Nature Structural and Molecular Biology, 22(5), 390-395. doi:10.1038/nsmb.3002.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-4102-4
Abstract
Recently, the first known light-driven sodium pumps, from the microbial rhodopsin family, were discovered. We have solved the structure of one of them, Krokinobacter eikastus ​rhodopsin 2 (​KR2), in the monomeric blue state and in two pentameric red states, at resolutions of 1.45 Å and 2.2 and 2.8 Å, respectively. The structures reveal the ion-translocation pathway and show that the sodium ion is bound outside the protein at the oligomerization interface, that the ion-release cavity is capped by a unique N-terminal α-helix and that the ion-uptake cavity is unexpectedly large and open to the surface. Obstruction of the cavity with the mutation G263F imparts ​KR2 with the ability to pump potassium. These results pave the way for the understanding and rational design of cation pumps with new specific properties valuable for optogenetics.