ArticleJournal of the American Chemical Society2010
Functional reconstitution of an ABC transporter in nanodiscs for use in electron paramagnetic resonance spectroscopy.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 86 citations in OpenAlex.
- Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025Article
- Bidirectional communication between nucleotide and substrate binding sites in a type IV multidrug ABC transporter.Nature communications · 2025Article
- Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024Article
- Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding.Structure (London, England : 1993) · 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
- Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.eLife · 2023Article
- Conformation of influenza AM2 membrane protein in nanodiscs and liposomes.Biochimica et biophysica acta. Biomembranes · 2023Article
- Substrate-bound and substrate-free outward-facing structures of a multidrug ABC exporter.Science advances · 2022Article
- Illumination of serotonin transporter mechanism and role of the allosteric site.Science advances · 2021Article
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- Correlating ion channel structure and function.Methods in enzymology · 2021Article
- Optimizing Targeted Inhibitors of P-Glycoprotein Using Computational and Structure-Guided Approaches.Journal of medicinal chemistry · 2019Article
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- The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019Article
- Structural basis for activation of voltage sensor domains in an ion channel TPC1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein.Biochemistry · 2018Article
- Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.The Journal of biological chemistry · 2018Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Biochemical characterization of essential cell division proteins FtsX and FtsE that mediate peptidoglycan hydrolysis by PcsB in Streptococcus pneumoniae.MicrobiologyOpen · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Electron paramagnetic resonance (EPR) spectroscopy is a powerful biophysical technique for study of the structural dynamics of membrane proteins. Many of these proteins interact with ligands or proteins on one or both sides of the membrane. Membrane proteins are typically reconstituted in proteoliposomes to observe their function in a physiologically relevant environment. However, membrane proteins can insert into liposomes in two different orientations, and surfaces facing the lumen of the vesicle can be inaccessible to ligands. This heterogeneity can lead to subpopulations that do not respond to ligand binding, complicating EPR spectral analysis, particularly for distance measurements. Using the well-characterized maltose transporter, an ATP binding cassette (ABC) transporter that interacts with ligands on both sides of the membrane, we provide evidence that reconstitution into nanodiscs, which are soluble disk-shaped phospholipid bilayers, is an ideal solution to these problems. We describe the functional reconstitution of the maltose transporter into nanodiscs and demonstrate that this system is ideally suited to study conformational changes and intramolecular distances by EPR.
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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.