Evidence map›Paper›PMID 31666521›Full record

ArticleNature communications2019

Unique structure and function of viral rhodopsins.

Dmitry Bratanov, Kirill Kovalev, Jan-Philipp Machtens, Roman Astashkin, Igor Chizhov, Dmytro Soloviov, Dmytro Volkov, Vitaly Polovinkin, Dmitrii Zabelskii, Thomas Mager and 19 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A dinoflagellate-infecting giant virus with a micron-length tail.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Mechanisms of inward transmembrane proton translocation.Nature structural & molecular biology · 2023
    Article
  14. Mirror proteorhodopsins.Communications chemistry · 2023
    Article
  15. Review
  16. Review
  17. Article
  18. Evolution of the Automatic Rhodopsin Modeling (ARM) Protocol.Topics in current chemistry (Cham) · 2022
    Review
  19. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  20. Searching Metagenomes for New Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

29 authors at 10 institutions in 6 countries.

Dmitry BratanovInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Kirill KovalevInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Jan-Philipp MachtensInstitute of Complex Systems (ICS), ICS-4: Zelluläre Biophysik, Forschungszentrum Jülich, Jülich, Germany.ORCID http://orcid.org/0000-0003-1673-8571
Roman AstashkinInstitut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-CEA-CNRS, Grenoble, France.
Igor ChizhovInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Dmytro SoloviovMoscow Institute of Physics and Technology, Dolgoprudniy, Russia.ORCID http://orcid.org/0000-0001-7945-2218
Dmytro VolkovInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Vitaly PolovinkinInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Dmitrii ZabelskiiInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.ORCID http://orcid.org/0000-0001-6906-975X
Thomas MagerMax Planck Institute of Biophysics, Frankfurt am Main, Germany.
Ivan GushchinMoscow Institute of Physics and Technology, Dolgoprudniy, Russia.ORCID http://orcid.org/0000-0002-5348-6070
Tatyana RokitskayaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia.ORCID http://orcid.org/0000-0002-7719-1875
Yuri AntonenkoBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia.
Alexey AlekseevInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Vitaly ShevchenkoInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Natalya YutinNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.
Riccardo RosselliEvolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, San Juan de Alicante, Spain.ORCID http://orcid.org/0000-0002-5832-2024
Christian BaekenInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Valentin BorshchevskiyInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Gleb BourenkovEuropean Molecular Biology Laboratory, Hamburg unit c/o DESY, Hamburg, Germany.ORCID http://orcid.org/0000-0002-2617-5920
Alexander PopovEuropean Synchrotron Radiation Facility, Grenoble, France.
Taras BalandinInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.
Georg BüldtMoscow Institute of Physics and Technology, Dolgoprudniy, Russia.
Dietmar J MansteinInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Francisco Rodriguez-ValeraEvolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, San Juan de Alicante, Spain.ORCID http://orcid.org/0000-0002-9809-2059
Christoph FahlkeMoscow Institute of Physics and Technology, Dolgoprudniy, Russia.
Ernst BambergMoscow Institute of Physics and Technology, Dolgoprudniy, Russia.
Eugene KooninNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0003-3943-8299
Valentin GordeliyInstitute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany. valentin.gordeliy@ibs.fr.
Moscow Institute of Physics and Technology · RUCentre National de la Recherche Scientifique · FRForschungszentrum Jülich · DELomonosov Moscow State University · RUMedizinische Hochschule Hannover · DENational Institutes of Health · USUniversitat de Miguel Hernández d'Elx · ESEuropean Molecular Biology Laboratory · DEEuropean Synchrotron Radiation Facility · FRMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

BacteriorhodopsinsCrystallography, X-RayHalobacterium salinarumIon Channel GatingIon ChannelsLightMolecular Dynamics SimulationPhycodnaviridaeProtein Structure, QuaternaryProtein Structure, TertiaryRhodopsins, MicrobialBacteriorhodopsinsIon ChannelsRhodopsins, Microbial

Identifiers

PMID31666521
PMCPMC6821725
OpenAlexW2982499955

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.