Evidence map›Paper›PMID 36086818›Full record

ArticleBiophysical journal2022

Spectroscopic and QM/MM studies of the Cu(I) binding site of the plant ethylene receptor ETR1.

George Cutsail, Stephan Schott-Verdugo, Lena Müller, Serena DeBeer, Georg Groth, Holger Gohlke

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biological formation of ethylene.RSC chemical biology · 2023
    Review
  5. Basis for high-affinity ethylene binding by the ethylene receptor ETR1 of Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

6 authors at 3 institutions in 1 country.

George CutsailMax Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany; Institute of Inorganic Chemistry, University of Duisburg-Essen, Universitätsstrasse 7, Essen, Germany.
Stephan Schott-VerdugoJohn von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), Institute of Biological Information Processing (IBI-7: Structural Bioinformatics), and Institute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich GmbH, Jülich, Germany.
Lena MüllerInstitut für Biochemische Pflanzenphysiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Serena DeBeerMax Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany.
Georg GrothInstitut für Biochemische Pflanzenphysiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Holger GohlkeJohn von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), Institute of Biological Information Processing (IBI-7: Structural Bioinformatics), and Institute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich GmbH, Jülich, Germany; Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany. Electronic address: gohlke@uni-duesseldorf.de.
Forschungszentrum Jülich · DEHeinrich Heine University Düsseldorf · DEMax Planck Institute for Chemical Energy Conversion · DE

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

Herein, we present, to our knowledge, the first spectroscopic characterization of the Cu(I) active site of the plant ethylene receptor ETR1. The x-ray absorption (XAS) and extended x-ray absorption fine structure (EXAFS) spectroscopies presented here establish that ETR1 has a low-coordinate Cu(I) site. The EXAFS resolves a mixed first coordination sphere of N/O and S scatterers at distances consistent with potential histidine and cysteine residues. This finding agrees with the coordination of residues C65 and H69 to the Cu(I) site, which are critical for ethylene activity and well conserved. Furthermore, the Cu K-edge XAS and EXAFS of ETR1 exhibit spectroscopic changes upon addition of ethylene that are attributed to modifications in the Cu(I) coordination environment, suggestive of ethylene binding. Results from umbrella sampling simulations of the proposed ethylene binding helix of ETR1 at a mixed quantum mechanics/molecular mechanics level agree with the EXAFS fit distance changes upon ethylene binding, particularly in the increase of the distance between H69 and Cu(I), and yield binding energetics comparable with experimental dissociation constants. The observed changes in the copper coordination environment might be the triggering signal for the transmission of the ethylene response.

Indexed as

CopperHistidineBinding SitesCysteineEthylenesReceptors, Cell SurfaceX-Ray Absorption SpectroscopyCopperCysteineEthylenesHistidineReceptors, Cell Surface

Identifiers

PMID36086818
PMCPMC9674993
OpenAlexW4295210856

What OpenQuestion holds

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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.