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7ZN3

Crystal structure of the light-driven inward proton pump xenorhodopsin BcXeR in the L state at pH 8.2 in the presence of sodium at 100K

Summary for 7ZN3
Entry DOI10.2210/pdb7zn3/pdb
Descriptorxenorhodopsin, EICOSANE, OLEIC ACID, ... (6 entities in total)
Functional Keywordsretinal, rhodopsin, xenorhodopsin, ion transport, isomerization, photocycle, membrane protein
Biological sourceBacillus coahuilensis
Total number of polymer chains3
Total formula weight93539.85
Authors
Kovalev, K.,Tsybrov, F.,Alekseev, A.,Bourenkov, G.,Gordeliy, V. (deposition date: 2022-04-20, release date: 2023-05-10, Last modification date: 2024-02-07)
Primary citationKovalev, K.,Tsybrov, F.,Alekseev, A.,Shevchenko, V.,Soloviov, D.,Siletsky, S.,Bourenkov, G.,Agthe, M.,Nikolova, M.,von Stetten, D.,Astashkin, R.,Bukhdruker, S.,Chizhov, I.,Royant, A.,Kuzmin, A.,Gushchin, I.,Rosselli, R.,Rodriguez-Valera, F.,Ilyinskiy, N.,Rogachev, A.,Borshchevskiy, V.,Schneider, T.R.,Bamberg, E.,Gordeliy, V.
Mechanisms of inward transmembrane proton translocation.
Nat.Struct.Mol.Biol., 30:970-979, 2023
Cited by
PubMed Abstract: Proton transport is indispensable for cell life. It is believed that molecular mechanisms of proton movement through different types of proton-conducting molecules have general universal features. However, elucidation of such mechanisms is a challenge. It requires true-atomic-resolution structures of all key proton-conducting states. Here we present a comprehensive function-structure study of a light-driven bacterial inward proton pump, xenorhodopsin, from Bacillus coahuilensis in all major proton-conducting states. The structures reveal that proton translocation is based on proton wires regulated by internal gates. The wires serve as both selectivity filters and translocation pathways for protons. The cumulative results suggest a general concept of proton translocation. We demonstrate the use of serial time-resolved crystallography at a synchrotron source with sub-millisecond resolution for rhodopsin studies, opening the door for principally new applications. The results might also be of interest for optogenetics since xenorhodopsins are the only alternative tools to fire neurons.
PubMed: 37386213
DOI: 10.1038/s41594-023-01020-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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