ArticleProceedings of the National Academy of Sciences of the United States of America1999
Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed.
- Cobamide Scavenging and Import via a Multiprotein Extracellular Relay in Bacteroides thetaiotaomicron.Chembiochem : a European journal of chemical biology · 2026Review
- Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V.Communications biology · 2025Article
- Article
- Multi-environment ecogenomics analysis of the cosmopolitan phylum Gemmatimonadota.Microbiology spectrum · 2023Article
- HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Metagenomic and chemical characterization of soil cobalamin production.The ISME journal · 2020Article
- Identification and detection ofHeliyon · 2019Article
- Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Article
- 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
- Allosteric Signaling Is Bidirectional in an Outer-Membrane Transport Protein.Biophysical journal · 2016Article
- A TonB-dependent receptor regulates antifungal HSAF biosynthesis in Lysobacter.Scientific reports · 2016Article
- ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition.Journal of bacteriology · 2016Review
- Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway.Journal of bacteriology · 2013Article
- 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
- The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization.Journal of bacteriology · 2012Article
- Identification of functionally important TonB-ExbD periplasmic domain interactions in vivo.Journal of bacteriology · 2012Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
Abstract
Transport of vitamin B(12) across the outer membrane of Escherichia coli, like that of iron-siderophore complexes, is an active transport process requiring a specific outer membrane transporter BtuB, the proton motive force, and the trans-periplasmic energy coupling protein TonB. Interaction between TonB and two of the TonB-dependent siderophore transporters has been detected previously by formaldehyde crosslinking. Here, site-directed disulfide crosslinking demonstrates contact between a conserved region of BtuB, called the TonB-box, and a portion of TonB, previously implicated as the site of suppressors of TonB-box mutations. The specific pattern of disulfide bonding to alternating residues in the TonB-box allowed deduction of the conformation and parallel orientation of the contact region between these two protein segments. Crosslinking at several positions was increased when BtuB was loaded with substrate, and the crosslinking pattern was altered by the presence of substitutions in BtuB that cause a TonB-uncoupled phenotype. This crosslinking process thus reflects protein interactions that are involved in coupling to active transport.
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