Evidence map›Paper›PMID 37162386›Full record

ArticleAngewandte Chemie (International ed. in English)2023

Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.

Samuel F Haysom, Jonathan Machin, James M Whitehouse, Jim E Horne, Katherine Fenn, Yue Ma, Hassane El Mkami, Nils Böhringer, Till F Schäberle, Neil A Ranson and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
13.2field-weighted citation impact, top 1% 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

28 citing papers in PubMed, 37 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

12 authors at 3 institutions in 2 countries.

Samuel F HaysomAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Jonathan MachinAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
James M WhitehouseAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Jim E HorneAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Katherine FennAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Yue MaAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Hassane El MkamiSchool of Physics and Astronomy, University of St. Andrews, St. Andrews, KY16 9SS, UK.
Nils BöhringerInstitute for Insect Biotechnology, Natural Product Research, Justus-Liebig-University Giessen, Ohlebergsweg 12, 35392, Giessen, Germany.
Till F SchäberleInstitute for Insect Biotechnology, Natural Product Research, Justus-Liebig-University Giessen, Ohlebergsweg 12, 35392, Giessen, Germany.
Neil A RansonAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
Sheena E RadfordAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-3079-8039
Christos PliotasAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-4309-4858
University of Leeds · GBJustus-Liebig-Universität Gießen · DEUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011151/1Biotechnology and Biological Sciences Research Council BB/S018069/1Biotechnology and Biological Sciences Research Council BB/W019795/1Medical Research Council MR/P018491/1Wellcome Trust 108466Wellcome Trust 108466/Z/15/ZWellcome Trust 221524Wellcome Trust 221524/Z/20/ZWellcome Trust 222373/Z/21/Z
6 · The paper itself

Abstract

The β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment.

Indexed as

Escherichia coliEscherichia coli ProteinsBacterial Outer Membrane ProteinsElectron Spin Resonance SpectroscopyPhenylpropionatesProtein FoldingBacterial Outer Membrane ProteinsdarobactinEscherichia coli ProteinsPhenylpropionatesBAMCryoemDarobactinIn-Cell EPRPELDOR

Identifiers

PMID37162386
PMCPMC10952311
OpenAlexW4376121194

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.