ArticleBiophysical journal2010
Conformational exchange in a membrane transport protein is altered in protein crystals.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Review
- A disulfide chaperone knockout facilitates spin labeling and pulse EPR spectroscopy of outer membrane transporters.Protein science : a publication of the Protein Society · 2023Article
- Lipids mediate supramolecular outer membrane protein assembly in bacteria.Science advances · 2022Article
- 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
- Evidence for the Supramolecular Organization of a Bacterial Outer-Membrane Protein from In Vivo Pulse Electron Paramagnetic Resonance Spectroscopy.Journal of the American Chemical Society · 2020Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Chasing the open-state structure of pentameric ligand-gated ion channels.The Journal of general physiology · 2017Article
- Natural Conformational Sampling of Human TNFα Visualized by Double Electron-Electron Resonance.Biophysical journal · 2017Article
- The Making and Breaking of a Substrate Trap.Biophysical journal · 2017Article
- Allosteric Signaling Is Bidirectional in an Outer-Membrane Transport Protein.Biophysical journal · 2016Article
- Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.Biochemistry · 2015Article
- Nanometer-scale water- and proton-diffusion heterogeneities across water channels in polymer electrolyte membranes.Angewandte Chemie (International ed. in English) · 2015Article
- Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.Methods in enzymology · 2015Article
- Closure of the cytoplasmic gate formed by TM5 and TM11 during transport in the oxalate/formate exchanger from Oxalobacter formigenes.Biochemistry · 2014Article
- Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Accounts of chemical research · 2014Review
- Conformational dynamics of ligand-dependent alternating access in LeuT.Nature structural & molecular biology · 2014Article
- The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Successful macromolecular crystallography requires solution conditions that may alter the conformational sampling of a macromolecule. Here, site-directed spin labeling is used to examine a conformational equilibrium within BtuB, the Escherichia coli outer membrane transporter for vitamin B(12). Electron paramagnetic resonance (EPR) spectra from a spin label placed within the N-terminal energy coupling motif (Ton box) of BtuB indicate that this segment is in equilibrium between folded and unfolded forms. In bilayers, substrate binding shifts this equilibrium toward the unfolded form; however, EPR spectra from this same spin-labeled mutant indicate that this unfolding transition is blocked in protein crystals. Moreover, crystal structures of this spin-labeled mutant are consistent with the EPR result. When the free energy difference between substates is estimated from the EPR spectra, the crystal environment is found to alter this energy by 3 kcal/mol when compared to the bilayer state. Approximately half of this energy change is due to solutes or osmolytes in the crystallization buffer, and the remainder is contributed by the crystal lattice. These data provide a quantitative measure of how a conformational equilibrium in BtuB is modified in the crystal environment, and suggest that more-compact, less-hydrated substates will be favored in protein crystals.
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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.