000865288 001__ 865288 000865288 005__ 20220930130219.0 000865288 0247_ $$2doi$$a10.1038/s41467-019-12718-0 000865288 0247_ $$2Handle$$a2128/23867 000865288 0247_ $$2altmetric$$aaltmetric:69508415 000865288 0247_ $$2pmid$$apmid:31666521 000865288 0247_ $$2WOS$$aWOS:000493275600013 000865288 037__ $$aFZJ-2019-04808 000865288 082__ $$a500 000865288 1001_ $$0P:(DE-Juel1)131964$$aGordeliy, Valentin$$b0$$eCorresponding author 000865288 245__ $$aUnique structure and function of viral rhodopsins 000865288 260__ $$a[London]$$bNature Publishing Group UK$$c2019 000865288 3367_ $$2DRIVER$$aarticle 000865288 3367_ $$2DataCite$$aOutput Types/Journal article 000865288 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1600089576_28885 000865288 3367_ $$2BibTeX$$aARTICLE 000865288 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000865288 3367_ $$00$$2EndNote$$aJournal Article 000865288 520__ $$aRecently, two groups of rhodopsin genes were identified in large double-stranded DNA viruses. The structure and function of viral rhodopsins are unknown. We present functional characterization and high-resolution structure of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII) of group 2. It forms a pentamer, with a symmetrical, bottle-like central channel with the narrow vestibule in the cytoplasmic part covered by a ring of 5 arginines, whereas 5 phenylalanines form a hydrophobic barrier in its exit. The proton donor E42 is placed in the helix B. The structure is unique among the known rhodopsins. Structural and functional data and molecular dynamics suggest that OLPVRII might be a light-gated pentameric ion channel analogous to pentameric ligand-gated ion channels, however, future patch clamp experiments should prove this directly. 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