8RSS

Crystal structure of marine actinobacteria clade rhodopsin (MAR) in the O* state

8RSS の概要

• エントリーDOI: 10.2210/pdb8rss/pdb
• 分子名称: Bacteriorhodopsin, OLEIC ACID, EICOSANE, ... (5 entities in total)
• 機能のキーワード: mac, macr, mar, proteorhodopsin, pr, xanthorodopsin, xr, membrane protein, xanthorhodopsin
• 由来する生物種: Candidatus Actinomarina minuta; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28516.91

構造登録者

Bukhdruker, S.,Kovalev, K.,Astashkin, R.,Gordeliy, V. (登録日: 2024-01-25, 公開日: 2025-04-02, 最終更新日: 2025-07-02)

主引用文献

Bukhdruker, S.,Gushchin, I.,Shevchenko, V.,Kovalev, K.,Polovinkin, V.,Tsybrov, F.,Astashkin, R.,Alekseev, A.,Mikhaylov, A.,Bukhalovich, S.,Bratanov, D.,Ryzhykau, Y.,Kuklina, D.,Caramello, N.,Rokitskaya, T.,Antonenko, Y.,Rulev, M.,Stoev, C.,Zabelskii, D.,Round, E.,Rogachev, A.,Borshchevskiy, V.,Ghai, R.,Bourenkov, G.,Zeghouf, M.,Cherfils, J.,Engelhard, M.,Chizhov, I.,Rodriguez-Valera, F.,Bamberg, E.,Gordeliy, V.
Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.
Sci Adv, 11:eadu5303-eadu5303, 2025

PubMed Abstract: Bacterial proton pumps, proteorhodopsins (PRs), are a major group of light-driven membrane proteins found in marine bacteria. They are functionally and structurally distinct from archaeal and eukaryotic proton pumps. To elucidate the proton transfer mechanism by PRs and understand the differences to nonbacterial pumps on a molecular level, high-resolution structures of PRs' functional states are needed. In this work, we have determined atomic-resolution structures of MAR, a PR from marine actinobacteria, in various functional states, notably the challenging late O intermediate state. These data and information from recent atomic-resolution structures on an archaeal outward proton pump bacteriorhodopsin and bacterial inward proton pump xenorhodopsin allow for deducing key universal elements for light-driven proton pumping. First, long hydrogen-bonded chains characterize proton pathways. Second, short hydrogen bonds allow proton storage and inhibit their backflow. Last, the retinal Schiff base is the active proton donor and acceptor to and from hydrogen-bonded chains.

PubMed: 40238873
DOI: 10.1126/sciadv.adu5303

実験手法

X-RAY DIFFRACTION (1.41 Å)