| Literature DB >> 25849142 |
Ivan Gushchin1, Vitaly Shevchenko2, Vitaly Polovinkin1, Kirill Kovalev3, Alexey Alekseev3, Ekaterina Round4, Valentin Borshchevskiy3, Taras Balandin4, Alexander Popov5, Thomas Gensch6, Christoph Fahlke6, Christian Bamann7, Dieter Willbold8, Georg Büldt9, Ernst Bamberg7, Valentin Gordeliy1.
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.Entities:
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Year: 2015 PMID: 25849142 DOI: 10.1038/nsmb.3002
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369