Evidence map›Paper›PMID 32034096›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

High-resolution structural insights into the heliorhodopsin family.

K Kovalev, D Volkov, R Astashkin, A Alekseev, I Gushchin, J M Haro-Moreno, I Chizhov, S Siletsky, M Mamedov, A Rogachev and 8 more

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Molecular properties of a viral heliorhodopsin, V2HeR2.Biophysics and physicobiology · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mirror proteorhodopsins.Communications chemistry · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors.

K KovalevInstitut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, 38000 Grenoble, France.
D VolkovInstitute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, 52428 Jülich, Germany.ORCID 0000-0003-2451-0091
R AstashkinInstitut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, 38000 Grenoble, France.
A AlekseevInstitute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, 52428 Jülich, Germany.
I GushchinResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
J M Haro-MorenoEvolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, 03202 San Juan de Alicante, Spain.
I ChizhovInstitute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.
S SiletskyBelozersky Institute of Physical-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.
M MamedovBelozersky Institute of Physical-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.
A RogachevResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
T BalandinInstitute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, 52428 Jülich, Germany.
V BorshchevskiyResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
A PopovStructural Biology Group, European Synchrotron Radiation Facility, 38000 Grenoble, France.
G BourenkovHamburg Unit care of Deutsches Elektronen-Synchrotron (DESY), European Molecular Biology Laboratory, 22607 Hamburg, Germany.
E BambergResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
F Rodriguez-ValeraResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
G BüldtResearch Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny 141701, Russia.
V GordeliyInstitut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, 38000 Grenoble, France; valentin.gordeliy@ibs.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 Å, which highlight its remarkable difference from all known rhodopsins. The interior of HeR's extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes.

Indexed as

Computational BiologyHydrogen-Ion ConcentrationModels, MolecularPhotolysisProtein ConformationRhodopsins, MicrobialRhodopsins, Microbialcrystal structuremembrane proteinretinalrhodopsinX-ray crystallography

Identifiers

PMID32034096
PMCPMC7049168

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LicenceCC BY-NC-ND
Read underepoch 390

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.