ArticleBiochemistry2012
The N-terminal domain of a TonB-dependent transporter undergoes a reversible stepwise denaturation.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- 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
- Going Outside the TonB Box: Identification of Novel FepA-TonB InteractionsJournal of bacteriology · 2017Article
- Gating of TonB-dependent transporters by substrate-specific forced remodelling.Nature communications · 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
- 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Gram-negative bacteria contain a family of outer membrane transport proteins that function in the uptake of rare nutrients, such as iron and vitamin B(12). These proteins are termed TonB-dependent because transport requires an interaction with the inner-membrane protein TonB. Using a combination of site-directed spin labeling and chemical denaturation, we examined the site-specific unfolding of regions of the Escherichia coli vitamin B(12) transporter, BtuB. The data indicate that a portion of the N-terminal region of the protein, which occupies the lumen of the BtuB barrel, denatures prior to the unfolding of the barrel and that the free energy of folding for the N-terminus is smaller than that typically seen for globular proteins. Moreover, the data indicate that the N-terminal domain does not unfold in a single event but unfolds in a series of independent steps. The unfolding of the N-terminus is reversible, and removal of denaturant restores the native fold of the protein. These data are consistent with proposed transport mechanisms that involve a transient rearrangement or unfolding of the N-terminus of the protein, and they provide evidence of a specific protein conformation that might be an intermediate accessed during transport.
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Registered trials
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