Evidence map›Paper›PMID 30948633›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.

Jakob Maciejko, Jagdeep Kaur, Johanna Becker-Baldus, Clemens Glaubitz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Resonant Mixing Dynamic Nuclear Polarization.The journal of physical chemistry letters · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  18. Review
  19. Article
  20. Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 1 institution in 1 country.

Jakob MaciejkoInstitute for Biophysical Chemistry, Goethe-University Frankfurt, 60438 Frankfurt, Germany.
Jagdeep KaurInstitute for Biophysical Chemistry, Goethe-University Frankfurt, 60438 Frankfurt, Germany.
Johanna Becker-BaldusInstitute for Biophysical Chemistry, Goethe-University Frankfurt, 60438 Frankfurt, Germany.ORCID 0000-0003-1995-7323
Clemens GlaubitzInstitute for Biophysical Chemistry, Goethe-University Frankfurt, 60438 Frankfurt, Germany; glaubitz@em.uni-frankfurt.de.ORCID 0000-0002-3554-6586
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteorhodopsin (PR) is a highly abundant, pentameric, light-driven proton pump. Proton transfer is linked to a canonical photocycle typical for microbial ion pumps. Although the PR monomer is able to undergo a full photocycle, the question arises whether the pentameric complex formed in the membrane via specific cross-protomer interactions plays a role in its functional mechanism. Here, we use dynamic nuclear polarization (DNP)-enhanced solid-state magic-angle spinning (MAS) NMR in combination with light-induced cryotrapping of photointermediates to address this topic. The highly conserved residue H75 is located at the protomer interface. We show that it switches from the (τ)- to the (π)-tautomer and changes its ring orientation in the M state. It couples to W34 across the oligomerization interface based on specific His/Trp ring orientations while stabilizing the pK

Indexed as

Rhodopsins, MicrobialHistidineIsomerismModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein SubunitsRepetitive Sequences, Amino AcidTryptophanHistidineProtein SubunitsproteorhodopsinRhodopsins, MicrobialTryptophanDNPNMRoligomerphotocycleproteorhodopsin

Identifiers

PMID30948633
PMCPMC6486740
OpenAlexW2934244368

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.