ArticleJournal of molecular biology2012
Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Bacterial TonB-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis.PLoS biology · 2024Article
- 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
- Conformational Differences Are Observed for the Active and Inactive Forms of Pinholin SThe journal of physical chemistry. B · 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
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- New Insights into the Regulation of Cell-Surface Signaling Activity Acquired from a Mutagenesis Screen of theFrontiers in microbiology · 2017Article
- Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.The Biochemical journal · 2016Article
- Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Accounts of chemical research · 2014Review
- Structural investigation of the transmembrane domain of KCNE1 in proteoliposomes.Biochemistry · 2014Article
- Interaction of a partially disordered antisigma factor with its partner, the signaling domain of the TonB-dependent transporter HasR.PloS one · 2014Article
- Use of electron paramagnetic resonance to solve biochemical problems.Biochemistry · 2013Review
- Anti-Sigma Factors in E. coli: Common Regulatory Mechanisms Controlling Sigma Factors Availability.Current genomics · 2013Article
- Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Outer-membrane TonB-dependent transporters, such as the Escherichia coli ferric citrate transporter FecA, interact with the inner-membrane protein TonB through an energy-coupling segment termed the Ton box. In FecA, which regulates its own transcription, the Ton box is preceded by an N-terminal extension that interacts with the inner-membrane protein FecR. Here, site-directed spin labeling was used to examine the structural basis for transcriptional signaling and Ton box regulation in FecA. EPR spectroscopy indicates that regions of the N-terminal domain are in conformational exchange, consistent with its role as a protein binding element; however, the local fold and dynamics of the domain are not altered by substrate or TonB. Distance restraints derived from pulse EPR were used to generate models for the position of the extension in the apo, substrate-, and TonB-bound states. In the apo state, this domain is positioned at the periplasmic surface of FecA, where it interacts with the Ton box and blocks access of the Ton box to the periplasm. Substrate addition rotates the transcriptional domain and exposes the Ton box, leading to a disorder transition in the Ton box that may facilitate interactions with TonB. When a soluble fragment of TonB is bound to FecA, the transcriptional domain is displaced to one edge of the barrel, consistent with a proposed β-strand exchange mechanism. However, neither substrate nor TonB displaces the N-terminus further into the periplasm. This result suggests that the intact TonB system mediates both signaling and transport by unfolding portions of the transporter.
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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.