ArticleBiophysics reports2017
Energy coupling mechanisms of AcrB-like RND transporters.
Article in Biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Conformational changes in the Niemann-Pick type C1 protein NCR1 drive sterol translocation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The energetics and ion coupling of cholesterol transport through Patched1.Science advances · 2023Article
- The Energetics and Ion Coupling of Cholesterol Transport Through Patched1.bioRxiv : the preprint server for biology · 2023Article
- AcrAB efflux pump impacts on the survival of adherent-invasive Escherichia coli strain LF82 inside macrophages.Scientific reports · 2023Article
- Insight into the AcrAB-TolC Complex Assembly Process Learned from Competition Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Probing the Dynamics of AcrB Through Disulfide Bond Formation.ACS omega · 2020Article
- Interplay between the electrostatic membrane potential and conformational changes in membrane proteins.Protein science : a publication of the Protein Society · 2019Review
- Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.Protein science : a publication of the Protein Society · 2018Review
- Thermodynamics of voltage-gated ion channels.Biophysics reports · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prokaryotic AcrB-like proteins belong to a family of transporters of the RND superfamily, and as main contributing factor to multidrug resistance pose a tremendous threat to future human health. A unique feature of AcrB transporters is the presence of two separate domains responsible for carrying substrate and generating energy. Significant progress has been made in elucidating the three-dimensional structures of the homo-trimer complexes of AcrB-like transporters, and a three-step functional rotation was identified for this class of transporters. However, the detailed mechanisms for the transduction of the substrate binding signal, as well as the energy coupling processes between the functionally distinct domains remain to be established. Here, we propose a model for the interdomain communication in AcrB that explains how the substrate binding signal from the substrate-carrier domain triggers protonation in the transmembrane domain. Our model further provides a plausible mechanism that explains how protonation induces conformational changes in the substrate-carrier domain. We summarize the thermodynamic principles that govern the functional cycle of the AcrB trimer complex.
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Registered trials
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