ArticleProtein science : a publication of the Protein Society2010
Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 39 citations in OpenAlex.
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- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein.International journal of molecular sciences · 2017Article
- Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.Protein science : a publication of the Protein Society · 2015Article
- Elastic deformation and area per lipid of membranes: atomistic view from solid-state deuterium NMR spectroscopy.Biochimica et biophysica acta · 2015Review
- 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
- The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.The Journal of biological chemistry · 2014Article
- Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.Biochemistry · 2014Article
- Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.Biophysical journal · 2013Article
- Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.Journal of molecular biology · 2012Article
- Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Applied magnetic resonance · 2012Article
- Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Biophysical journal · 2012Article
- Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Biochemistry · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Site-directed spin labeling (SDSL) was used to investigate local structure and conformational exchange in two bacterial outer-membrane TonB-dependent transporters, BtuB and FecA. Protecting osmolytes, such as polyethylene glycols (PEGs) are known to modulate a substrate-dependent conformational equilibrium in the energy coupling motif (Ton box) of BtuB. Here, we demonstrate that a segment that is N-terminal to the Ton box in BtuB, is in conformational exchange between ordered and disordered states with or without substrate. Protecting osmolytes shift this equilibrium to favor the more ordered, folded state. However, a segment of BtuB that is C-terminal to the Ton box that is not solvent exposed is insensitive to PEGs. Protecting osmolytes also modulate a conformational equilibrium in the Ton box of FecA, with larger molecular weight PEGs producing the largest shifts in the conformational free energy. These data indicate that solvent-exposed regions of these transporters undergo conformational exchange and that regions of these transporters that are involved in protein-protein interactions sample multiple conformational substates. The sensitivity to solute provides an explanation for differences seen between two high-resolution structures of BtuB, which each likely represent one conformation from a subset of states that are normally sampled by the protein. This work also illustrates how SDSL and osmolytes may be used to characterize and quantitate conformational equilibria in membrane proteins.
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