Evidence map›Paper›PMID 39428489›Full record

ArticleNature communications2024

Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling.

Ruojing Zhang, Kevin L Jagessar, Matthew Brownd, Adithya Polasa, Richard A Stein, Mahmoud Moradi, Erkan Karakas, Hassane S Mchaourab

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
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.

Ruojing ZhangDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0002-9637-3762
Kevin L JagessarDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0003-1475-2513
Matthew BrowndDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA.
Adithya PolasaDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA.ORCID 0000-0002-7764-6585
Richard A SteinDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0002-0541-7150
Mahmoud MoradiDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA.ORCID 0000-0002-0601-402X
Erkan KarakasDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA.ORCID 0000-0001-6552-3185
Hassane S MchaourabDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, USA. hassane.mchaourab@vanderbilt.edu.ORCID 0000-0002-5673-0980

Funding

Thermo Scientific Glacios cryo-TEMS10OD030292 · OD · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2021 to 2021
$2.0M
Structural Dynamics of Active TransportersR35GM152382 · NIGMS · VANDERBILT UNIVERSITY · PI Hassane S Mchaourab · 2024 to 2026
$1.7M
Physics-based characterization of functionally relevant protein conformational dynamicsR35GM147423 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI Mahmoud Moradi · 2022 to 2026
$1.7M
Structural dynamics of peptide-translocating ABC transportersR01GM128087 · NIGMS · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 2019 to 2022
$1.7M
NIGMS NIH HHS R01 GM128087NIGMS NIH HHS R35 GM147423NIGMS NIH HHS R35 GM152382NIH HHS S10 OD030292
6 · The paper itself

Abstract

Protease-containing ABC transporters (PCATs) couple the energy of ATP hydrolysis to the processing and export of diverse cargo proteins across cell membranes to mediate antimicrobial resistance and quorum sensing. Here, we combine biochemical analysis, single particle cryoEM, and DEER spectroscopy in lipid bilayers along with computational analysis to illuminate the structural and energetic underpinnings of coupled cargo protein export. Our integrated investigation uncovers competitive interplay between nucleotides and cargo protein binding that ensures the latter's orderly processing and subsequent transport. The energetics of cryoEM structures in lipid bilayers are congruent with the inferred mechanism from ATP turnover analysis and reveal a snapshot of a high-energy outward-facing conformation that provides an exit pathway into the lipid bilayer and/or the extracellular side. DEER investigation of the core ABC transporter suggests evolutionary tuning of the energetic landscape to fulfill the function of substrate processing prior to export.

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersCryoelectron MicroscopyLipid BilayersBacterial ProteinsModels, MolecularNanostructuresPeptide HydrolasesProtein BindingProtein ConformationAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsLipid BilayersPeptide Hydrolases

Identifiers

PMID39428489
PMCPMC11491471

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.