ArticleProceedings of the National Academy of Sciences of the United States of America2003
Differential substrate-induced signaling through the TonB-dependent transporter BtuB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- Can Vitamin B12 Assist the Internalization of Antisense LNA Oligonucleotides into Bacteria?Antibiotics (Basel, Switzerland) · 2021Article
- Going Outside the TonB Box: Identification of Novel FepA-TonB InteractionsJournal of bacteriology · 2017Article
- From Homodimer to Heterodimer and Back: Elucidating the TonB Energy Transduction Cycle.Journal of bacteriology · 2015Article
- Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Biochemistry · 2013Article
- Mobility of BtuB and OmpF in the Escherichia coli outer membrane: implications for dynamic formation of a translocon complex.Biophysical journal · 2010Article
- Swimming against the tide: progress and challenges in our understanding of colicin translocation.Nature reviews. Microbiology · 2010Review
- Identification of meningococcal genes necessary for colonization of human upper airway tissue.Infection and immunity · 2009Article
- Membrane hydrocarbon thickness modulates the dynamics of a membrane transport protein.Biophysical journal · 2008Article
- Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane.Journal of bacteriology · 2008Article
- Molecular basis for substrate-dependent transmembrane signaling in an outer-membrane transporter.Journal of molecular biology · 2007Article
- Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Deletion and substitution analysis of the Escherichia coli TonB Q160 region.Journal of bacteriology · 2007Article
- Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.The EMBO journal · 2007Article
- Evidence of ball-and-chain transport of ferric enterobactin through FepA.The Journal of biological chemistry · 2007Article
- Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance.Biochemistry · 2006Article
- Solutes modify a conformational transition in a membrane transport protein.Biophysical journal · 2006Article
- Identification of the iron-responsive genes of Neisseria gonorrhoeae by microarray analysis in defined medium.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The BtuB transporter mediates high-affinity binding and TonB-dependent active transport of vitamin B12 [cyanocobalamin (CNCbl)] across the outer membrane of Escherichia coli. A characteristic feature of TonB-dependent transporters is the Ton box, a conserved sequence near the N terminus and exposed to the periplasm. Crosslinking to TonB and site-directed spin labeling indicated that the Ton box of BtuB undergoes a substantial conformational transition in response to CNCbl binding, but only slight movement was seen in crystal structures. An in vivo method of detecting substrate-induced changes in the Ton box environment measured reaction of a biotin maleimide derivative with cysteine substitutions through the N-terminal region of BtuB between positions 1 and 31. The degree of maleimide labeling of different residues correlated with their accessibility in the crystal structure. Labeling of many positions was increased strongly when CNCbl was present, consistent with the undocking of this region proposed from spin-labeling analyses. The receptor-binding domain of colicin E3, which binds to BtuB competitively with CNCbl, resulted in decreased labeling. Both substrate-induced transitions occur in and beyond the Ton box and were affected by transport-uncoupling substitutions. Thus, two transport substrates that bind competitively to the extracellular face of BtuB stabilize opposite transitions of the Ton box.
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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.