Evidence map›Paper›PMID 29712846›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Ribosome protection by antibiotic resistance ATP-binding cassette protein.

Weixin Su, Veerendra Kumar, Yichen Ding, Rya Ero, Aida Serra, Benjamin Sian Teck Lee, Andrew See Weng Wong, Jian Shi, Siu Kwan Sze, Liang Yang and 1 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

69 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  3. Review
  4. [Molecular mechanisms underlying the development and spread of antibiotic resistance].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2026
    Review
  5. Article
  6. Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
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  20. Article

9 more citing papers are in PubMed but not listed here.

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.

Weixin SuSchool of Biological Sciences, Nanyang Technological University, Singapore 637551.
Veerendra KumarInstitute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore 138673.
Yichen DingSingapore Centre for Environmental Life Sciences Engineering, Nanyang Technological University, Singapore 637551.
Rya EroSchool of Biological Sciences, Nanyang Technological University, Singapore 637551; ygao@ntu.edu.sg yangliang@ntu.edu.sg rero@ntu.edu.sg.
Aida SerraSchool of Biological Sciences, Nanyang Technological University, Singapore 637551.
Benjamin Sian Teck LeeSchool of Biological Sciences, Nanyang Technological University, Singapore 637551.
Andrew See Weng WongInstitute of Structural Biology, Nanyang Technological University, Singapore 639798.
Jian ShiCentre for BioImaging Sciences, National University of Singapore, Singapore 117557.
Siu Kwan SzeSchool of Biological Sciences, Nanyang Technological University, Singapore 637551.
Liang YangSchool of Biological Sciences, Nanyang Technological University, Singapore 637551; ygao@ntu.edu.sg yangliang@ntu.edu.sg rero@ntu.edu.sg.ORCID 0000-0002-2362-0128
Yong-Gui GaoSchool of Biological Sciences, Nanyang Technological University, Singapore 637551; ygao@ntu.edu.sg yangliang@ntu.edu.sg rero@ntu.edu.sg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosome is one of the richest targets for antibiotics. Unfortunately, antibiotic resistance is an urgent issue in clinical practice. Several ATP-binding cassette family proteins confer resistance to ribosome-targeting antibiotics through a yet unknown mechanism. Among them, MsrE has been implicated in macrolide resistance. Here, we report the cryo-EM structure of ATP form MsrE bound to the ribosome. Unlike previously characterized ribosomal protection proteins, MsrE is shown to bind to ribosomal exit site. Our structure reveals that the domain linker forms a unique needle-like arrangement with two crossed helices connected by an extended loop projecting into the peptidyl-transferase center and the nascent peptide exit tunnel, where numerous antibiotics bind. In combination with biochemical assays, our structure provides insight into how MsrE binding leads to conformational changes, which results in the release of the drug. This mechanism appears to be universal for the ABC-F type ribosome protection proteins.

Indexed as

Drug Resistance, MicrobialAdenosine TriphosphateAnti-Bacterial AgentsATP-Binding Cassette TransportersBacteriaBacterial ProteinsBinding SitesCrystallography, X-RayModels, MolecularPeptidyl TransferasesProtein BiosynthesisProtein ConformationRibosomesAdenosine TriphosphateAnti-Bacterial AgentsATP-Binding Cassette TransportersBacterial ProteinsPeptidyl TransferasesABC-Fantibiotic resistanceMsrEprotein synthesisribosome protection

Identifiers

PMID29712846
PMCPMC5960329

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.