Evidence map›Paper›PMID 34193947›Full record

ArticleCommunications biology2021

Structure-based insights into evolution of rhodopsins.

Dmitrii Zabelskii, Natalia Dmitrieva, Oleksandr Volkov, Vitaly Shevchenko, Kirill Kovalev, Taras Balandin, Dmytro Soloviov, Roman Astashkin, Egor Zinovev, Alexey Alekseev and 12 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  3. Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. Modified Rhodopsins FromFrontiers in molecular biosciences · 2021
    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

22 authors at 6 institutions in 5 countries.

Dmitrii Zabelskii *Institute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.ORCID 0000-0001-6906-975X
Natalia Dmitrieva *Institut für Biologische Informationsprozesse - Molekular- und Zellphysiologie (IBI-1),Forschungszentrum Jülich, Jülich, Germany.
Oleksandr Volkov *Institute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Vitaly Shevchenko *Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Kirill KovalevResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Taras BalandinInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Dmytro SoloviovResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.ORCID 0000-0001-7945-2218
Roman AstashkinResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Egor ZinovevInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Alexey AlekseevInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Ekaterina RoundInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Vitaly PolovinkinInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.
Igor ChizhovInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Andrey RogachevResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Ivan OkhrimenkoResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Valentin BorshchevskiyInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany.ORCID 0000-0003-4398-9712
Vladimir ChupinResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Georg BüldtResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Natalia YutinNational Center for Biotechnology Information, National Library of Medicine, National Institutesof Health, Bethesda, MD, United States.ORCID 0000-0002-3633-5123
Ernst BambergMax Planck Institute of Biophysics, Frankfurt am Main, Germany.
Eugene KooninNational Center for Biotechnology Information, National Library of Medicine, National Institutesof Health, Bethesda, MD, United States.ORCID 0000-0003-3943-8299
Valentin GordeliyInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), ForschungszentrumJülich, Jülich, Germany. valentin.gordeliy@ibs.fr.ORCID 0000-0001-5782-5896
Moscow Institute of Physics and Technology · RUCentre National de la Recherche Scientifique · FRForschungszentrum Jülich · DENational Institutes of Health · USMax Planck Institute of Biophysics · DEMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rhodopsins, most of which are proton pumps generating transmembrane electrochemical proton gradients, span all three domains of life, are abundant in the biosphere, and could play a crucial role in the early evolution of life on earth. Whereas archaeal and bacterial proton pumps are among the best structurally characterized proteins, rhodopsins from unicellular eukaryotes have not been well characterized. To fill this gap in the current understanding of the proton pumps and to gain insight into the evolution of rhodopsins using a structure-based approach, we performed a structural and functional analysis of the light-driven proton pump LR (Mac) from the pathogenic fungus Leptosphaeria maculans. The first high-resolution structure of fungi rhodopsin and its functional properties reveal the striking similarity of its membrane part to archaeal but not to bacterial rhodopsins. We show that an unusually long N-terminal region stabilizes the protein through direct interaction with its extracellular loop (ECL2). We compare to our knowledge all available structures and sequences of outward light-driven proton pumps and show that eukaryotic and archaeal proton pumps, most likely, share a common ancestor.

Indexed as

Ion TransportLightPhylogenyProtein DomainsProton PumpsRhodopsinProton PumpsRhodopsin

Identifiers

PMID34193947
PMCPMC8245419
OpenAlexW3175429273

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.