ArticleProceedings of the National Academy of Sciences of the United States of America2007
Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- A disulfide chaperone knockout facilitates spin labeling and pulse EPR spectroscopy of outer membrane transporters.Protein science : a publication of the Protein Society · 2023Article
- Structural intermediates observed only in intacteLife · 2021Article
- Disulfide Chaperone Knockouts Enable In Vivo Double Spin Labeling of an Outer Membrane Transporter.Biophysical journal · 2019Article
- The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.Nature communications · 2019Article
- Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- New insights into iron acquisition by cyanobacteria: an essential role for ExbB-ExbD complex in inorganic iron uptake.The ISME journal · 2015Article
- The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.The Journal of biological chemistry · 2014Article
- Continuous wave W- and D-band EPR spectroscopy offer "sweet-spots" for characterizing conformational changes and dynamics in intrinsically disordered proteins.Biochemical and biophysical research communications · 2014Article
- Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Biochemistry · 2013Article
- Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.Journal of molecular biology · 2012Article
- Direct evidence that the carboxyl-terminal sequence of a bacterial chemoreceptor is an unstructured linker and enzyme tether.Protein science : a publication of the Protein Society · 2011Article
- Characterization of the disordered-to-α-helical transition of IA₃ by SDSL-EPR spectroscopy.Protein science : a publication of the Protein Society · 2011Article
- Conformational exchange in a membrane transport protein is altered in protein crystals.Biophysical journal · 2010Article
- Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins.Protein science : a publication of the Protein Society · 2010Article
- TonB-dependent transporters: regulation, structure, and function.Annual review of microbiology · 2010Review
- Coordination chemistry of bacterial metal transport and sensing.Chemical reviews · 2009Review
- FhuA (TonA), the career of a protein.Journal of bacteriology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Site-directed spin labeling (SDSL) was used to examine and compare transmembrane signaling events in the bacterial outer-membrane transport proteins BtuB, FecA, and FhuA. These proteins extract energy for transport by coupling to the transperiplasmic protein TonB, an interaction that is thought to be mediated by the Ton box, a highly conserved energy-coupling motif in these transporters. In the ferric citrate transporter, FecA, SDSL indicates that the Ton box undergoes a substrate-induced disorder transition similar to that seen for BtuB, the vitamin B(12) transporter. This conformational change produces an aqueous exposed, highly disordered protein fragment, which likely regulates transporter-TonB interactions. However, in the ferrichrome transporter, FhuA, SDSL does not reveal a substrate-induced unfolding transition. In this protein, with or without substrate, the Ton box conformation is found to be highly dynamic and constitutively unfolded. In addition, SDSL indicates that structural features seen in high-resolution models are not found in membrane-associated FhuA. Taken together, these data indicate that the Ton box of FhuA may always be available for interactions with TonB, implying that transporter-TonB interactions in FhuA are either constitutive or not regulated by the Ton box configuration.
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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.