Evidence map›Paper›PMID 41370088›Full record

ArticlemBio2026

Cryo-EM reveals the structural heterogeneity and conformational flexibility of multidrug efflux pumps MdtB and MdtF.

Surekha Padmanaban, Clayton Fernando Rencilin, Rupam Biswas, Somnath Dutta

Abstract read
In one paragraph

Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–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

1 citing paper in PubMed.

  1. 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

4 authors.

Surekha PadmanabanMolecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.ORCID 0000-0003-1411-4028
Clayton Fernando RencilinMolecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.ORCID 0000-0001-6949-4000
Rupam BiswasMolecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.
Somnath DuttaMolecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.ORCID 0000-0002-3181-0108

Funding

Anusandhan National Research Foundation India CRG/ 2022/002674, SERB-STR/2022/000006DBT/Wellcome Trust India Alliance IA/E/19/1/504978Department of Biotechnology, Ministry of Science and Technology, India BT/INF/22/SP22844/2017Department of Science and Technology, Ministry of Science and Technology, India SR/FST/LSII-039/2015Wellcome Trust
6 · The paper itself

Abstract

Resistance-nodulation-cell division (RND) efflux pumps are the major cause of multidrug resistance in bacteria, particularly in Gram-negative bacteria. They are complex molecular machines forming tripartite assemblies that actively transport out a wide range of antimicrobial agents, including antibiotics, biocides, and host defense molecules. However, the presence of multiple RND transporters with overlapping functions in a single bacterium raises questions about their individual functional relevance. In this study, we determined the cryo-electron microscopy (cryo-EM) structures of two distinct hydrophobic and amphiphilic efflux (HAE)-RND transporters from IMPORTANCE: Resistance-nodulation-cell division (RND) efflux pumps are mainly responsible for multidrug resistance by extruding a wide range of antibiotics from bacterial cells. These pumps are frequently overexpressed in multidrug-resistant

Indexed as

Escherichia coliEscherichia coli ProteinsMembrane Transport ProteinsCryoelectron MicroscopyDrug Resistance, Multiple, BacterialModels, MolecularProtein ConformationEscherichia coli ProteinsMembrane Transport ProteinsCryo-EMdetergentE. coliefflux pumpsMdtBMdtFmembrane protein

Identifiers

PMID41370088
PMCPMC12802153

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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.