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Mechanisms of inward transmembrane proton translocation

Nature structural & molecular biology, 2023-07, Vol.30 (7), p.970-979 [Peer Reviewed Journal]

2023. The Author(s), under exclusive licence to Springer Nature America, Inc. ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-023-01020-9 ;PMID: 37386213

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Title:
Mechanisms of inward transmembrane proton translocation
Author: Kovalev, Kirill ; Tsybrov, Fedor ; Alekseev, Alexey ; Shevchenko, Vitaly ; Soloviov, Dmytro ; Siletsky, Sergey ; Bourenkov, Gleb ; Agthe, Michael ; Nikolova, Marina ; von Stetten, David ; Astashkin, Roman ; Bukhdruker, Sergey ; Chizhov, Igor ; Royant, Antoine ; Kuzmin, Alexander ; Gushchin, Ivan ; Rosselli, Riccardo ; Rodriguez-Valera, Francisco ; Ilyinskiy, Nikolay ; Rogachev, Andrey ; Borshchevskiy, Valentin ; Schneider, Thomas R ; Bamberg, Ernst ; Gordeliy, Valentin
Subjects: Cell membranes ; Crystallography ; Genetics ; Information processing ; Ion Transport ; Life Sciences ; Molecular modelling ; Optics ; Proton Pumps ; Protons ; Rhodopsin ; Structure-function relationships ; Synchrotrons ; Translocation
Is Part Of: Nature structural & molecular biology, 2023-07, Vol.30 (7), p.970-979
Description: 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.
Publisher: United States: Nature Publishing Group
Language: English
Identifier: ISSN: 1545-9993
EISSN: 1545-9985
DOI: 10.1038/s41594-023-01020-9
PMID: 37386213
Source: Hyper Article en Ligne (HAL) (Open Access)

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Mechanisms of inward transmembrane proton translocation

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