Evidence map›Paper›PMID 37550453›Full record

ArticleNature structural & molecular biology2023

Structural conservation of antibiotic interaction with ribosomes.

Helge Paternoga, Caillan Crowe-McAuliffe, Lars V Bock, Timm O Koller, Martino Morici, Bertrand Beckert, Alexander G Myasnikov, Helmut Grubmüller, Jiří Nováček, Daniel N Wilson

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
13.7field-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

47 citing papers in PubMed, 89 citations in OpenAlex.

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  17. ACS chemical biology · 2026
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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

10 authors at 4 institutions in 3 countries.

Helge Paternoga *Institute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.
Caillan Crowe-McAuliffe *Institute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.
Lars V BockTheoretical and Computational Biophysics Department, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID http://orcid.org/0000-0003-4554-7336
Timm O KollerInstitute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.ORCID http://orcid.org/0000-0003-0145-4891
Martino MoriciInstitute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.ORCID http://orcid.org/0000-0002-7304-5264
Bertrand BeckertDubochet Center for Imaging at EPFL-UNIL, Batiment Cubotron, Lausanne, Switzerland.
Alexander G MyasnikovDubochet Center for Imaging at EPFL-UNIL, Batiment Cubotron, Lausanne, Switzerland.ORCID http://orcid.org/0000-0003-2607-7121
Helmut GrubmüllerTheoretical and Computational Biophysics Department, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID http://orcid.org/0000-0002-3270-3144
Jiří NováčekCentral European Institute of Technology (CEITEC), Masaryk University, Brno, Czech Republic.ORCID http://orcid.org/0000-0003-4013-3898
Daniel N WilsonInstitute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany. Daniel.Wilson@chemie.uni-hamburg.de.ORCID http://orcid.org/0000-0003-3816-3828
Universität Hamburg · DEÉcole Polytechnique Fédérale de Lausanne · CHMax Planck Institute for Multidisciplinary SciencesCentral European Institute of Technology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosome is a major target for clinically used antibiotics, but multidrug resistant pathogenic bacteria are making our current arsenal of antimicrobials obsolete. Here we present cryo-electron-microscopy structures of 17 distinct compounds from six different antibiotic classes bound to the bacterial ribosome at resolutions ranging from 1.6 to 2.2 Å. The improved resolution enables a precise description of antibiotic-ribosome interactions, encompassing solvent networks that mediate multiple additional interactions between the drugs and their target. Our results reveal a high structural conservation in the binding mode between antibiotics with the same scaffold, including ordered water molecules. Water molecules are visualized within the antibiotic binding sites that are preordered, become ordered in the presence of the drug and that are physically displaced on drug binding. Insight into RNA-ligand interactions will facilitate development of new antimicrobial agents, as well as other RNA-targeting therapies.

Indexed as

Anti-Bacterial AgentsRibosomesBacteriaBinding SitesRNAAnti-Bacterial AgentsRNA

Identifiers

PMID37550453
PMCPMC10497419
OpenAlexW4385638623

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.