期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-12718-0
关键词
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资金
- Agence Nationale de la Recherche (ANR), France
- Deutsche Forschungsgemeinschaft (DFG), Germany [ANR-15-CE11-0029-02/FA 301/11-1]
- DFG [FOR 2518, MA 7525/1-1]
- Frankfurt: Cluster of Excellence Frankfurt Macromolecular Complexes by the Max Planck Society
- Commissariat a l'Energie Atomique et aux Energies Alternatives (Institut de Biologie Structurale)-Helmholtz-Gemeinschaft Deutscher Forschungszentren (Forschungszentrum Julich) Special Terms and Conditions 5.1 specific agreement
- Grenoble Instruct-ERIC center (ISBG) [UMS 3518 CNRS-CEA-UJF-EMBL]
- FRISBI [ANR-10-INBS-05-02]
- GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- RSF-DFG grant (Helmholtz-RSF Joint Research Groups grant (RSF)) [19-44-06302]
- AEI/FEDER, EU [VIREVO CGL2016-76273-P]
- Deutsche Forschungsgemeinschaft under Germany's Excellence Strategy [EXC 2155, 39087428]
- Intramural Research Program of the National Institutes of Health of the USA
- Ministry of Science and Higher Education of the Russian Federation [6.9909.2017/6.7]
- Russian Foundation for Basic Research [17-00-00164komfi]
- Ministry of Science and High Education of the Russian Federation [6.3157.2017]
- [ANR-14-CE09-0028]
- Russian Science Foundation [19-44-06302] Funding Source: Russian Science Foundation
Recently, 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. The data shed light on a fundamentally distinct branch of rhodopsins and may contribute to the understanding of virus-host interactions in ecologically important marine protists.
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