![Microorganisms | Free Full-Text | TonB-Dependent Transporters in Sphingomonads: Unraveling Their Distribution and Function in Environmental Adaptation | HTML Microorganisms | Free Full-Text | TonB-Dependent Transporters in Sphingomonads: Unraveling Their Distribution and Function in Environmental Adaptation | HTML](https://www.mdpi.com/microorganisms/microorganisms-08-00359/article_deploy/html/images/microorganisms-08-00359-g001-550.jpg)
Microorganisms | Free Full-Text | TonB-Dependent Transporters in Sphingomonads: Unraveling Their Distribution and Function in Environmental Adaptation | HTML
![Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes | PNAS Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes | PNAS](https://www.pnas.org/content/106/51/21990/F1.large.jpg)
Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes | PNAS
![TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health](https://cdnsciencepub.com/cms/10.1139/O10-141/asset/images/large/o10-141f3.jpeg)
TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health
![Substrate-induced exposure of an energy-coupling motif of a membrane transporter | Nature Structural & Molecular Biology Substrate-induced exposure of an energy-coupling motif of a membrane transporter | Nature Structural & Molecular Biology](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2F73309/MediaObjects/41594_2000_Article_BFnsb0300_205_Fig5_HTML.gif)
Substrate-induced exposure of an energy-coupling motif of a membrane transporter | Nature Structural & Molecular Biology
![New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?: Trends in Biochemical Sciences New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?: Trends in Biochemical Sciences](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/591627/4552415/gr1.jpg)
New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?: Trends in Biochemical Sciences
![Frontiers | Application of TonB-Dependent Transporters in Vaccine Development of Gram-Negative Bacteria | Cellular and Infection Microbiology Frontiers | Application of TonB-Dependent Transporters in Vaccine Development of Gram-Negative Bacteria | Cellular and Infection Microbiology](https://www.frontiersin.org/files/Articles/589115/fcimb-10-589115-HTML/image_m/fcimb-10-589115-g002.jpg)
Frontiers | Application of TonB-Dependent Transporters in Vaccine Development of Gram-Negative Bacteria | Cellular and Infection Microbiology
![Interactions between the Outer Membrane Ferric Citrate Transporter FecA and TonB: Studies of the FecA TonB Box | Journal of Bacteriology Interactions between the Outer Membrane Ferric Citrate Transporter FecA and TonB: Studies of the FecA TonB Box | Journal of Bacteriology](https://journals.asm.org/cms/10.1128/JB.185.6.1870-1885.2003/asset/70050255-1df1-4b2c-9b20-8059c5b7c61f/assets/graphic/jb0631307002.jpeg)
Interactions between the Outer Membrane Ferric Citrate Transporter FecA and TonB: Studies of the FecA TonB Box | Journal of Bacteriology
![A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs42003-019-0676-z/MediaObjects/42003_2019_676_Fig5_HTML.png)
A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology
![Interactions of the FhuA Ton box with the C-terminal domain of TonB.... | Download Scientific Diagram Interactions of the FhuA Ton box with the C-terminal domain of TonB.... | Download Scientific Diagram](https://www.researchgate.net/profile/Cezar-Khursigara-2/publication/7042093/figure/fig2/AS:669244807184399@1536571804677/Interactions-of-the-FhuA-Ton-box-with-the-C-terminal-domain-of-TonB-A-The-interprotein_Q640.jpg)
Interactions of the FhuA Ton box with the C-terminal domain of TonB.... | Download Scientific Diagram
![New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? - ScienceDirect New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0968000408001011-gr1b1.jpg)
New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? - ScienceDirect
![Predicting the Complex Structure and Functional Motions of the Outer Membrane Transporter and Signal Transducer FecA: Biophysical Journal Predicting the Complex Structure and Functional Motions of the Outer Membrane Transporter and Signal Transducer FecA: Biophysical Journal](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/2039878136/2053471272/gr1.jpg)
Predicting the Complex Structure and Functional Motions of the Outer Membrane Transporter and Signal Transducer FecA: Biophysical Journal
![Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex. | Semantic Scholar Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/5dfa94b57cef7c4669c3c6846e96ae7486913232/1-Figure1-1.png)
Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex. | Semantic Scholar
![A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs42003-019-0676-z/MediaObjects/42003_2019_676_Fig3_HTML.png)
A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound | Communications Biology
![TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health](https://cdnsciencepub.com/cms/10.1139/O10-141/asset/images/large/o10-141f2.jpeg)
TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health
![TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health](https://cdnsciencepub.com/cms/10.1139/O10-141/asset/images/large/o10-141f1.jpeg)
TonB or not TonB: is that the question? This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health
![Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter | PNAS Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter | PNAS](https://www.pnas.org/content/pnas/96/19/10673/F1.large.jpg)
Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter | PNAS
The TonB box. (A) Sequence alignments of TonB boxes. Shown are sequence... | Download Scientific Diagram
![Gating of TonB-dependent transporters by substrate-specific forced remodelling | Nature Communications Gating of TonB-dependent transporters by substrate-specific forced remodelling | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fncomms14804/MediaObjects/41467_2017_Article_BFncomms14804_Fig1_HTML.jpg)
Gating of TonB-dependent transporters by substrate-specific forced remodelling | Nature Communications
![Ternary structure of the outer membrane transporter FoxA with resolved signalling domain provides insights into TonB-mediated siderophore uptake | eLife Ternary structure of the outer membrane transporter FoxA with resolved signalling domain provides insights into TonB-mediated siderophore uptake | eLife](https://iiif.elifesciences.org/lax/48528%2Felife-48528-fig2-v2.tif/full/1500,/0/default.jpg)
Ternary structure of the outer membrane transporter FoxA with resolved signalling domain provides insights into TonB-mediated siderophore uptake | eLife
![Ternary structure of the outer membrane transporter FoxA with resolved signalling domain provides insights into TonB-mediated siderophore uptake | eLife Ternary structure of the outer membrane transporter FoxA with resolved signalling domain provides insights into TonB-mediated siderophore uptake | eLife](https://iiif.elifesciences.org/lax/48528%2Felife-48528-fig1-v2.tif/full/1500,/0/default.jpg)