Evidence map›Paper›PMID 32703899›Full record

ArticleThe Journal of biological chemistry2020

The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants.

Jessica E Besaw, Wei-Lin Ou, Takefumi Morizumi, Bryan T Eger, Juan D Sanchez Vasquez, Jessica H Y Chu, Andrew Harris, Leonid S Brown, R J Dwayne Miller, Oliver P Ernst

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Protonation-Enhanced Energy Transfer in Xanthorhodopsin Kin4B8.The journal of physical chemistry letters · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mutations conferring SOScientific reports · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. Article
  14. Unique ClBiophysics and physicobiology · 2021
    Article
  15. 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

10 authors at 2 institutions in 1 country.

Jessica E BesawDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada.
Wei-Lin OuDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Takefumi MorizumiDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Bryan T EgerDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Juan D Sanchez VasquezDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada; Department of Immunology, University of Toronto, Toronto, Ontario, Canada.
Jessica H Y ChuDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Andrew HarrisDepartment of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
Leonid S BrownDepartment of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
R J Dwayne MillerDepartment of Chemistry, University of Toronto, Toronto, Ontario, Canada; Department of Physics, University of Toronto, Toronto, Ontario, Canada.
Oliver P ErnstDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada. Electronic address: oliver.ernst@utoronto.ca.
University of Toronto · CAUniversity of Guelph · CA

Funding

High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
NIH HHS S10 OD012289
6 · The paper itself

Abstract

Microbial rhodopsins are versatile and ubiquitous retinal-binding proteins that function as light-driven ion pumps, light-gated ion channels, and photosensors, with potential utility as optogenetic tools for altering membrane potential in target cells. Insights from crystal structures have been central for understanding proton, sodium, and chloride transport mechanisms of microbial rhodopsins. Two of three known groups of anion pumps, the archaeal halorhodopsins (HRs) and bacterial chloride-pumping rhodopsins, have been structurally characterized. Here we report the structure of a representative of a recently discovered third group consisting of cyanobacterial chloride and sulfate ion-pumping rhodopsins, the

Indexed as

MutationBinding SitesBiopolymersCrystallography, X-RayCyanobacteriaIon TransportProtein ConformationProton PumpsProtonsRetinaldehydeRhodopsins, MicrobialBiopolymersProton PumpsProtonsRetinaldehydeRhodopsins, Microbialbacteriorhodopsinbicelle crystallizationchloride pumpchloride transportcyanobacterial rhodopsinfunctional conversionfunctional interconversionMastigocladopsis repensmembrane proteinmicrobial rhodopsinprotein structureproton pumpretinal proteinstructure–functionX-ray crystallography

Identifiers

PMID32703899
PMCPMC7606686
OpenAlexW3045442280

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.