Abstract
Abstract
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.
Funder
Deutsche Forschungsgemeinschaft
Agence Nationale de la Recherche
Russian Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Reference80 articles.
1. Oesterhelt, D. & Stoeckenius, W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat. New Biol. 233, 149–152 (1971).
2. Shalaeva, D. N., Galperin, M. Y. & Mulkidjanian, A. Y. Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins. Biol. Direct 10, 63 (2015).
3. Béjà, O. & Lanyi, J. K. Nature’s toolkit for microbial rhodopsin ion pumps. Proc. Natl Acad. Sci. USA 111, 6538–6539 (2014).
4. Ernst, O. P. et al. Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem. Rev. 114, 126–163 (2014).
5. Gushchin, I. et al. Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria. J. Am. Chem. Soc. 3, 12631–12636 (2013).
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