Evidence map›Paper›PMID 23872846›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria.

Ivan Gushchin, Pavel Chervakov, Pavel Kuzmichev, Alexander N Popov, Ekaterina Round, Valentin Borshchevskiy, Andrii Ishchenko, Lada Petrovskaya, Vladimir Chupin, Dmitry A Dolgikh and 4 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 97 citations in OpenAlex.

  1. Special Issue "Ion Pumps: Molecular Mechanisms, Structure, Physiology".International journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mirror proteorhodopsins.Communications chemistry · 2023
    Article
  10. Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023
    Article
  11. Review
  12. Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Arseniev, Alexander A [corrected to Arseniev, Alexander S]
5 · Who and what money

Authors and funding

14 authors at 7 institutions in 3 countries.

Ivan GushchinInstitut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes, 38027 Grenoble, France.
Pavel Chervakov
Pavel Kuzmichev
Alexander N Popov
Ekaterina Round
Valentin Borshchevskiy
Andrii Ishchenko
Lada Petrovskaya
Vladimir Chupin
Dmitry A Dolgikh
Alexander S Arseniev
Alexander A Arseniev
Mikhail Kirpichnikov
Valentin Gordeliy
Forschungszentrum Jülich · DERussian Academy of Sciences · RUInstitute of Bioorganic Chemistry · RUCentre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FRLomonosov Moscow State University · RUMoscow Institute of Physics and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light-driven proton pumps are present in many organisms. Here, we present a high-resolution structure of a proteorhodopsin from a permafrost bacterium, Exiguobacterium sibiricum rhodopsin (ESR). Contrary to the proton pumps of known structure, ESR possesses three unique features. First, ESR's proton donor is a lysine side chain that is situated very close to the bulk solvent. Second, the α-helical structure in the middle of the helix F is replaced by 3(10)- and π-helix-like elements that are stabilized by the Trp-154 and Asn-224 side chains. This feature is characteristic for the proteorhodopsin family of proteins. Third, the proton release region is connected to the bulk solvent by a chain of water molecules already in the ground state. Despite these peculiarities, the positions of water molecule and amino acid side chains in the immediate Schiff base vicinity are very well conserved. These features make ESR a very unusual proton pump. The presented structure sheds light on the large family of proteorhodopsins, for which structural information was not available previously.

Indexed as

BacillaceaeBacterial ProteinsCrystallography, X-RayProtein Structure, SecondaryProtein Structure, TertiaryRhodopsinRhodopsins, MicrobialStructure-Activity RelationshipBacterial ProteinsproteorhodopsinRhodopsinRhodopsins, Microbialbacteriorhodopsinphotocycleretinalretinylidene protein

Identifiers

PMID23872846
PMCPMC3732926
OpenAlexW1994152613

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.