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  Unique structure and function of viral rhodopsins

Bratanov, D., Kovalev, K., Machtens, J.-P., Astashkin, R., Chizhov, I., Soloviov, D., et al. (2019). Unique structure and function of viral rhodopsins. Nature Communications, 10: 4939. doi:10.1038/s41467-019-12718-0.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-0CD2-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-0CD3-0
Genre: Journal Article

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 Creators:
Bratanov, Dmitry1, 2, 3, Author
Kovalev, Kirill1, 2, 3, 4, 5, 6, Author
Machtens, Jan-Philipp6, 7, Author
Astashkin, Roman3, 4, Author
Chizhov, Igor8, Author
Soloviov, Dmytro4, 9, 10, 11, Author
Volkov, Dmytro1, 2, 4, Author
Polovinkin, Vitaly1, 3, Author
Zabelskii, Dmitrii1, 2, 4, Author
Mager, Thomas12, Author              
Gushchin, Ivan4, Author
Rokitskaya, Tatyana13, Author
Antonenko, Yuri13, Author
Alekseev, Alexey1, 2, 4, 5, Author
Shevchenko, Vitaly1, 2, 4, 5, Author
Yutin, Natalya14, Author
Rosselli, Riccardo15, Author
Baeken, Christian1, 2, Author
Borshchevskiy, Valentin1, 2, 4, Author
Bourenkov, Gleb16, Author
Popov, Alexander17, AuthorBalandin, Taras1, 2, AuthorBüldt, Georg4, AuthorManstein, Dietmar J.8, AuthorRodriguez-Valera, Francisco15, AuthorFahlke, Christoph4, 6, AuthorBamberg, Ernst12, Author              Koonin, Eugene14, AuthorGordeliy, Valentin1, 2, 3, 4, Author more..
Affiliations:
1Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany, ou_persistent22              
2JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, Germany, ou_persistent22              
3Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-CEA-CNRS, Grenoble, France, ou_persistent22              
4Moscow Institute of Physics and Technology, Dolgoprudniy, Russia, ou_persistent22              
5Institute of Crystallography, University of Aachen (RWTH), Aachen, Germany, ou_persistent22              
6Institute of Complex Systems (ICS), ICS-4: Zelluläre Biophysik, Forschungszentrum Jülich, Jülich, Germany, ou_persistent22              
7Department of Molecular Pharmacology, University of Aachen (RWTH), Aachen, Germany, ou_persistent22              
8Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany, ou_persistent22              
9Joint Institute for Nuclear Research, Dubna, Russia, ou_persistent22              
10Taras Shevchenko National University of Kyiv, Kyiv, Ukraine, ou_persistent22              
11Institute for Safety Problems of Nuclear Power Plants NASof Ukraine, Chornobyl, Kyiv Region, Kyiv, Ukraine, ou_persistent22              
12Emeritusgruppe Biophysikalische Chemie, Max Planck Institute of Biophysics, Max Planck Society, ou_2253652              
13Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia, ou_persistent22              
14National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA, ou_persistent22              
15Evolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, San Juan de Alicante, Spain, ou_persistent22              
16European Molecular Biology Laboratory, Hamburg unit c/o DESY, Hamburg, Germany, ou_persistent22              
17European Synchrotron Radiation Facility, Grenoble, France, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2019-03-262019-09-162019-10-30
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-019-12718-0
BibTex Citekey: bratanov_unique_2019
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 10 Sequence Number: 4939 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723