Evidence map›Paper›PMID 41744473›Full record

ArticleActa crystallographica. Section F, Structural biology communications2026

Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain.

Jiye Wang, Kenta Tsutsumi, Mika Hirose, Ryosuke Nakashima, Takayuki Kato, Kunihiko Nishino, Atsushi Nakagawa, Eiki Yamashita

Abstract read
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In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Jiye WangLaboratory for Supramolecular Crystallography, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0009-0002-2512-7713
Kenta TsutsumiLaboratory for Supramolecular Crystallography, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-1168-6656
Mika HiroseLaboratory for High Resolution Cryo-EM, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0001-8991-587X
Ryosuke NakashimaBiomolecular Science and Regulation Department, SANKEN, The University of Osaka, Ibaraki, Osaka 567-0047, Japan.
Takayuki KatoLaboratory for High Resolution Cryo-EM, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-8879-6685
Kunihiko NishinoBiomolecular Science and Regulation Department, SANKEN, The University of Osaka, Ibaraki, Osaka 567-0047, Japan.
Atsushi NakagawaLaboratory for Supramolecular Crystallography, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-1700-7861
Eiki YamashitaLaboratory for Supramolecular Crystallography, Institute for Protein Research, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-4278-0039

Funding

Japan Science and Technology Agency JPMJSP2138Japan Society for the Promotion of Science 21K19337Japan Society for the Promotion of Science 23K23822
6 · The paper itself

Abstract

RND-type multidrug-efflux pumps are major contributors to multidrug resistance in Gram-negative bacteria, with MexY from Pseudomonas aeruginosa playing a central role in aminoglycoside resistance. Unlike other RND transporters, MexY exhibits unusually large open clefts in the binding and extrusion states. To determine whether this feature is intrinsic to its drug-recognition porter domain, we created a chimeric protein, MexBYB, by replacing the funnel-like and transmembrane domains of MexY with those of the homologous transporter MexB, and determined its structures by cryoEM under apo and kanamycin-supplemented conditions. Under both conditions, MexBYB was reported to adopt symmetric-like and asymmetric conformations. Structural comparisons reveal that the unusually large open clefts are retained in MexBYB, indicating that this feature is intrinsic to the MexY porter domain.

Indexed as

Bacterial ProteinsCryoelectron MicroscopyGram-Negative BacteriaRecombinant Fusion ProteinsBacterial Outer Membrane ProteinsEscherichia coliMembrane Transport ProteinsModels, MolecularProtein DomainsBacterial Outer Membrane ProteinsBacterial ProteinsMembrane Transport ProteinsMexB protein, Pseudomonas aeruginosaRecombinant Fusion Proteinscryo-EMdrug-efflux transportersmembrane proteinsPseudomonas aeruginosa

Identifiers

PMID41744473
PMCPMC12961675

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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.