Evidence map›Paper›PMID 31467343›Full record

ArticleScientific reports2019

Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels.

Eliane H Yardeni, Thorsten Bahrenberg, Richard A Stein, Smriti Mishra, Elia Zomot, Bim Graham, Kellie L Tuck, Thomas Huber, Eitan Bibi, Hassane S Mchaourab and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
8.0field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

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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

11 authors at 4 institutions in 3 countries.

Eliane H YardeniDepartment of Biomolecular Sciences, Weizmann Institute of Science Rehovot, Rehovot, 76100, Israel.
Thorsten BahrenbergDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, 76100, Israel.
Richard A SteinDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.
Smriti MishraDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.
Elia ZomotDepartment of Biomolecular Sciences, Weizmann Institute of Science Rehovot, Rehovot, 76100, Israel.
Bim GrahamMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, 3052, Australia.
Kellie L TuckSchool of Chemistry, Monash University, Wellington Road, Clayton, Victoria, Australia.
Thomas HuberResearch School of Chemistry, The Australian National University, Canberra, ACT 2601, Australia.
Eitan BibiDepartment of Biomolecular Sciences, Weizmann Institute of Science Rehovot, Rehovot, 76100, Israel. eitan.bibi@weizmann.ac.il.
Hassane S MchaourabDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA. hassane.mchaourab@vanderbilt.edu.
Daniella GoldfarbDepartment of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, 76100, Israel. Daniella.goldfarb@weizmann.ac.il.ORCID http://orcid.org/0000-0001-5714-7159
Weizmann Institute of Science · ILVanderbilt University · USMonash University · AUAustralian National University · AU

Funding

Structural Dynamics of Multi-drug TransportersR01GM077659 · NIGMS · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 2006 to 2023
$5.0M
NIGMS NIH HHS R01 GM077659
6 · The paper itself

Abstract

Methodological and technological advances in EPR spectroscopy have enabled novel insight into the structural and dynamic aspects of integral membrane proteins. In addition to an extensive toolkit of EPR methods, multiple spin labels have been developed and utilized, among them Gd(III)-chelates which offer high sensitivity at high magnetic fields. Here, we applied a dual labeling approach, employing nitroxide and Gd(III) spin labels, in conjunction with Q-band and W-band double electron-electron resonance (DEER) measurements to characterize the solution structure of the detergent-solubilized multidrug transporter MdfA from E. coli. Our results identify highly flexible regions of MdfA, which may play an important role in its functional dynamics. Comparison of distance distribution of spin label pairs on the periplasm with those calculated using inward- and outward-facing crystal structures of MdfA, show that in detergent micelles, the protein adopts a predominantly outward-facing conformation, although more closed than the crystal structure. The cytoplasmic pairs suggest a small preference to the outward-facing crystal structure, with a somewhat more open conformation than the crystal structure. Parallel DEER measurements with the two types of labels led to similar distance distributions, demonstrating the feasibility of using W-band spectroscopy with a Gd(III) label for investigation of the structural dynamics of membrane proteins.

Indexed as

CytoplasmElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsGadoliniumMembrane Transport ProteinsNitrogen OxidesProtein ConformationEscherichia coli ProteinsGadoliniumMdfa protein, E coliMembrane Transport ProteinsNitrogen Oxidesnitroxyl

Identifiers

PMID31467343
PMCPMC6715713
OpenAlexW2970099993

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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.