Evidence map›Paper›PMID 31594941›Full record

ArticleNature communications2019

Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition.

Dmitrii Y Travin, Zoe L Watson, Mikhail Metelev, Fred R Ward, Ilya A Osterman, Irina M Khven, Nelli F Khabibullina, Marina Serebryakova, Peter Mergaert, Yury S Polikanov and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-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

44 citing papers in PubMed, 68 citations in OpenAlex.

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  11. Isolation and Characterization of Lactic Acid Bacteria From "International journal of microbiology · 2025
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  19. Enterolyin S, a Polythiazole-containing Hemolytic Peptide from Enterococcus caccae.Chembiochem : a European journal of chemical biology · 2024
    Article
  20. 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

12 authors at 7 institutions in 4 countries.

Dmitrii Y TravinCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.ORCID http://orcid.org/0000-0003-0189-0159
Zoe L WatsonDepartment of Chemistry, University of California, Berkeley, USA.ORCID http://orcid.org/0000-0002-4877-7914
Mikhail MetelevCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.ORCID http://orcid.org/0000-0003-2829-6395
Fred R WardDepartment of Molecular and Cell Biology, University of California, Berkeley, USA.
Ilya A OstermanCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.
Irina M KhvenDepartment of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
Nelli F KhabibullinaDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0001-7319-1272
Marina SerebryakovaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia.ORCID http://orcid.org/0000-0002-5402-8215
Peter MergaertInstitute for Integrative Biology of the Cell (I2BC), CNRS CEA University Paris-Sud, University Paris-Saclay, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0002-5919-7317
Yury S PolikanovDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL, USA. yuryp@uic.edu.ORCID http://orcid.org/0000-0002-5064-0327
Jamie H D CateDepartment of Chemistry, University of California, Berkeley, USA. jcate@lbl.gov.ORCID http://orcid.org/0000-0001-5965-7902
Konstantin SeverinovCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia. severik@waksman.rutgers.edu.
University of California, Berkeley · USLomonosov Moscow State University · RUSkolkovo Institute of Science and Technology · RUUniversity of Illinois Chicago · USCentre National de la Recherche Scientifique · FRRutgers, The State University of New Jersey · USUppsala University · SE

Funding

Molecular mechanisms of action of ribosome-targeting antibiotics.R01GM132302 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI POLIKANOV, YURY · 2019 to 2022
$1.3M
Repurposing the Ribosome for Exotic PolymersR01GM114454 · NIGMS · YALE UNIVERSITY · PI SCHEPARTZ, ALANNA · 2017 to 2019
$1.1M
Structural basis of Erm-mediated macrolide resistanceR21AI137584 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MANKIN, ALEXANDER S, POLIKANOV, YURY · 2018 to 2019
$440k
NIAID NIH HHS R21 AI137584NIGMS NIH HHS R01 GM114454NIGMS NIH HHS R01 GM132302
6 · The paper itself

Abstract

Ribosome-synthesized post-translationally modified peptides (RiPPs) represent a rapidly expanding class of natural products with various biological activities. Linear azol(in)e-containing peptides (LAPs) comprise a subclass of RiPPs that display outstanding diversity of mechanisms of action while sharing common structural features. Here, we report the discovery of a new LAP biosynthetic gene cluster in the genome of Rhizobium Pop5, which encodes the precursor peptide and modification machinery of phazolicin (PHZ) - an extensively modified peptide exhibiting narrow-spectrum antibacterial activity against some symbiotic bacteria of leguminous plants. The cryo-EM structure of the Escherichia coli 70S-PHZ complex reveals that the drug interacts with the 23S rRNA and uL4/uL22 proteins and obstructs ribosomal exit tunnel in a way that is distinct from other compounds. We show that the uL4 loop sequence determines the species-specificity of antibiotic action. PHZ expands the known diversity of LAPs and may be used in the future as biocontrol agent for agricultural needs.

Indexed as

Anti-Bacterial AgentsAzolesBiological Control AgentsCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsMicrobial Sensitivity TestsMultigene FamilyPeptide BiosynthesisPeptidesPhaseolusProtein BiosynthesisRhizobiumRibosomal ProteinsRibosomesRNA, Ribosomal, 23SAnti-Bacterial AgentsAzolesBiological Control AgentsEscherichia coli ProteinsPeptidesRibosomal ProteinsRNA, Ribosomal, 23S

Identifiers

PMID31594941
PMCPMC6783444
OpenAlexW2979595179

What OpenQuestion holds

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LicenceCC BY
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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.