6EYU
Crystal structure of the inward H(+) pump xenorhodopsin
Summary for 6EYU
Entry DOI | 10.2210/pdb6eyu/pdb |
Descriptor | Bacteriorhodopsin, RETINAL, EICOSANE, ... (5 entities in total) |
Functional Keywords | retinal protein, proton transport, membrane protein |
Biological source | Nanosalina sp. (strain J07AB43) |
Total number of polymer chains | 3 |
Total formula weight | 88515.04 |
Authors | Kovalev, K.,Shevchenko, V.,Polovinkin, V.,Mager, T.,Gushchin, I.,Melnikov, I.,Borshchevskiy, V.,Popov, A.,Alekseev, A.,Gordeliy, V. (deposition date: 2017-11-13, release date: 2017-12-13, Last modification date: 2024-10-16) |
Primary citation | Shevchenko, V.,Mager, T.,Kovalev, K.,Polovinkin, V.,Alekseev, A.,Juettner, J.,Chizhov, I.,Bamann, C.,Vavourakis, C.,Ghai, R.,Gushchin, I.,Borshchevskiy, V.,Rogachev, A.,Melnikov, I.,Popov, A.,Balandin, T.,Rodriguez-Valera, F.,Manstein, D.J.,Bueldt, G.,Bamberg, E.,Gordeliy, V. Inward H(+) pump xenorhodopsin: Mechanism and alternative optogenetic approach. Sci Adv, 3:e1603187-, 2017 Cited by PubMed Abstract: Generation of an electrochemical proton gradient is the first step of cell bioenergetics. In prokaryotes, the gradient is created by outward membrane protein proton pumps. Inward plasma membrane native proton pumps are yet unknown. We describe comprehensive functional studies of the representatives of the yet noncharacterized xenorhodopsins from Nanohaloarchaea family of microbial rhodopsins. They are inward proton pumps as we demonstrate in model membrane systems, cells, human embryonic kidney cells, neuroblastoma cells, and rat hippocampal neuronal cells. We also solved the structure of a xenorhodopsin from the nanohalosarchaeon (XeR) and suggest a mechanism of inward proton pumping. We demonstrate that the XeR is a powerful pump, which is able to elicit action potentials in rat hippocampal neuronal cells up to their maximal intrinsic firing frequency. Hence, inwardly directed proton pumps are suitable for light-induced remote control of neurons, and they are an alternative to the well-known cation-selective channelrhodopsins. PubMed: 28948217DOI: 10.1126/sciadv.1603187 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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