ArticleProceedings of the National Academy of Sciences of the United States of America2017
Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 84 citations in OpenAlex.
- ATP-driven conformational dynamics reveal hidden intermediates in a heterodimeric ABC transporter.eLife · 2026Article
- Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.Nature communications · 2026Article
- Molecular mechanism of substrate transport by human peroxisomal ABCD3.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure and mechanism of a mycobacterial isoniazid efflux pump MsRv1273c/72c with a degenerate nucleotide-binding site.Nature communications · 2025Article
- Mechanistic Insights Revealed by YbtPQ in the Occluded State.Biomolecules · 2024Article
- The transport activity of the multidrug ABC transporter BmrA does not require a wide separation of the nucleotide-binding domains.The Journal of biological chemistry · 2024Article
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- The Alternating Access Mechanism in Mammalian Multidrug Resistance Transporters and Their Bacterial Homologs.Membranes · 2023Article
- The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase.Nature communications · 2022Article
- Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.Biomolecular NMR assignments · 2022Article
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle.Science advances · 2021Article
- Evidence for the Involvement of Pleckstrin Homology Domain-Containing Proteins in the Transport of Enterocin DD14 (EntDD14); a Leaderless Two-Peptide Bacteriocin.International journal of molecular sciences · 2021Article
- Optimization of Membrane Protein TmrA Purification Procedure Guided by Analytical Ultracentrifugation.Membranes · 2021Article
- A Conserved Motif in Intracellular Loop 1 Stabilizes the Outward-Facing Conformation of TmrAB.Journal of molecular biology · 2021Article
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Uncurtaining the pivotal role of ABC transporters in diabetes mellitus.Environmental science and pollution research international · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
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Authors and funding
17 authors at 5 institutions in 3 countries.
Funding
Abstract
ABC transporters form one of the largest protein superfamilies in all domains of life, catalyzing the movement of diverse substrates across membranes. In this key position, ABC transporters can mediate multidrug resistance in cancer therapy and their dysfunction is linked to various diseases. Here, we describe the 2.7-Å X-ray structure of heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), which not only shares structural homology with the antigen translocation complex TAP, but is also able to restore antigen processing in human TAP-deficient cells. TmrAB exhibits a broad peptide specificity and can concentrate substrates several thousandfold, using only one single active ATP-binding site. In our structure, TmrAB adopts an asymmetric inward-facing state, and we show that the C-terminal helices, arranged in a zipper-like fashion, play a crucial role in guiding the conformational changes associated with substrate transport. In conclusion, TmrAB can be regarded as a model system for asymmetric ABC exporters in general, and for TAP in particular.
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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.