ArticleBiochemistry2006
Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Electron paramagnetic resonance spectroscopic characterization of the human KCNE3 protein in lipodisq nanoparticles for structural dynamics of membrane proteins.Biophysical chemistry · 2023Article
- A disulfide chaperone knockout facilitates spin labeling and pulse EPR spectroscopy of outer membrane transporters.Protein science : a publication of the Protein Society · 2023Article
- HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural intermediates observed only in intacteLife · 2021Article
- Vitamin BBiophysical journal · 2021Article
- Extracellular loops of BtuB facilitate transport of vitamin B12 through the outer membrane of E. coli.PLoS computational biology · 2020Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Characterization of the Human KCNQ1 Voltage Sensing Domain (VSD) in Lipodisq Nanoparticles for Electron Paramagnetic Resonance (EPR) Spectroscopic Studies of Membrane Proteins.The journal of physical chemistry. B · 2020Article
- PELDOR/DEER: An Electron Paramagnetic Resonance Method to Study Membrane Proteins in Lipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Disulfide Chaperone Knockouts Enable In Vivo Double Spin Labeling of an Outer Membrane Transporter.Biophysical journal · 2019Article
- Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels.Scientific reports · 2019Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Site-Directed Spin Labeling EPR for Studying Membrane Proteins.BioMed research international · 2018Review
- Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Biophysical journal · 2017Article
- Allosteric Signaling Is Bidirectional in an Outer-Membrane Transport Protein.Biophysical journal · 2016Article
- Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts.Physical chemistry chemical physics : PCCP · 2016Article
- EPR and NMR spectroscopies provide input on the coordination of Cu(I) and Ag(I) to a disordered methionine segment.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Room-temperature distance measurements of immobilized spin-labeled protein by DEER/PELDOR.Biophysical journal · 2015Article
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4 authors.
Funding
Abstract
BtuB is a TonB-dependent transport protein that binds and carries vitamin B(12) across the outer membrane of Gram negative bacteria such as Escherichia coli. Previous work has demonstrated that the Ton box, a highly conserved segment near the N-terminus of the protein, undergoes an order-to-disorder transition upon the binding of substrate. Here, we incorporate pairs of nitroxide spin labels into membrane reconstituted BtuB and utilize a four-pulse double electron-electron resonance (DEER) experiment to measure distances between the Ton box and the periplasmic surface of the transporter with and without substrate. During reconstitution, the labeled membrane protein was diluted with wild-type protein, which significantly reduced the intermolecular electron spin-spin relaxation rate and increased the DEER signal-to-noise ratio. In the absence of substrate, each spin pair gives rise to a single distribution of distances that is consistent with the crystal structure obtained for BtuB; however, distances that are much longer are found in the presence of substrate, and the data are consistent with the existence of an equilibrium between folded and unfolded states of the Ton box. From these distances, a model for the position of the Ton box was constructed, and it indicates that the N-terminal end of the Ton box extends approximately 20 to 30 A into the periplasm upon the addition of substrate. We propose that this substrate-induced extension provides the signal that initiates interactions between BtuB and the inner membrane protein TonB.
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