ArticleeLife2020
A single power stroke by ATP binding drives substrate translocation in a heterodimeric ABC transporter.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- ATP-driven conformational dynamics reveal hidden intermediates in a heterodimeric ABC transporter.eLife · 2026Article
- Capturing transient states of heterodimeric ABC transporter TM287/288 by time-resolved small-angle X-ray scattering.Biophysical journal · 2026Article
- Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.Nature communications · 2026Article
- Predictive modelling of the COMATOSE transporter reveals a conserved ligand binding pocket for acyl-CoAs.Scientific reports · 2026Article
- Molecular mechanism of substrate transport by human peroxisomal ABCD3.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nucleotide asymmetry and flexible linker dynamics modulate drug efflux cycle of P-glycoprotein, A computational study.Computational and structural biotechnology journal · 2025Article
- Interdomain communication in a homodimeric ABC transporter.The Journal of biological chemistry · 2024Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
- ABC Transporters in Bacterial Nanomachineries.International journal of molecular sciences · 2023Review
- Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1.Nature communications · 2022Article
- Effects of Exogenous ATP on Melanoma Growth and Tumor Metabolism in C57BL/6 Mice.Comparative medicine · 2022Article
- Metalloprotein-Specific or Critical Amino Acid Residues: Perspectives on Plant-Precise Detoxification and Recognition Mechanisms under Cadmium Stress.International journal of molecular sciences · 2022Review
- Optimization of Membrane Protein TmrA Purification Procedure Guided by Analytical Ultracentrifugation.Membranes · 2021Article
- Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease.Nature communications · 2021Article
- A Conserved Motif in Intracellular Loop 1 Stabilizes the Outward-Facing Conformation of TmrAB.Journal of molecular biology · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Article
- Single Cell-like Systems Reveal Active Unidirectional and Light-Controlled Transport by Nanomachineries.ACS nano · 2021Article
- Quantitative real-time analysis of the efflux by the MacAB-TolC tripartite efflux pump clarifies the role of ATP hydrolysis within mechanotransmission mechanism.Communications biology · 2021Article
- Enzymatic trans-bilayer lipid transport: Mechanisms, efficiencies, slippage, and membrane curvature.Biochimica et biophysica acta. Biomembranes · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ATP-binding cassette (ABC) transporters constitute the largest family of primary active transporters, responsible for many physiological processes and human maladies. However, the mechanism how chemical energy of ATP facilitates translocation of chemically diverse compounds across membranes is poorly understood. Here, we advance the quantitative mechanistic understanding of the heterodimeric ABC transporter TmrAB, a functional homolog of the transporter associated with antigen processing (TAP) by single-turnover analyses at single-liposome resolution. We reveal that a single conformational switch by ATP binding drives unidirectional substrate translocation. After this power stroke, ATP hydrolysis and phosphate release launch the return to the resting state, which facilitates nucleotide exchange and a new round of substrate binding and translocation. In contrast to hitherto existing steady-state assays, our single-turnover approach uncovers the power stroke in substrate translocation and the tight chemomechanical coupling in these molecular machines.
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Registered trials
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.