ArticleProceedings of the National Academy of Sciences of the United States of America2006
Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 78 citations in OpenAlex.
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- A Paired Database of Predicted and Experimental Protein Peptide Binding Information.Scientific data · 2025Article
- Discovery of a Pseudomonas aeruginosa-specific small molecule targeting outer membrane protein OprH-LPS interaction by a multiplexed screen.Cell chemical biology · 2025Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Colicin E1 opens its hinge to plug TolC.eLife · 2022Article
- Force-Generation by the Trans-Envelope Tol-Pal System.Frontiers in microbiology · 2022Review
- Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.The EMBO journal · 2021Article
- The molecular interplay of the establishment of an infection - gene expression of Diaphorina citri gut and Candidatus Liberibacter asiaticus.BMC genomics · 2021Article
- Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.Nature communications · 2020Article
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Article
- Structural and biophysical analysis of nuclease protein antibiotics.The Biochemical journal · 2016Article
- Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.The Journal of biological chemistry · 2016Review
- ZnO nanoparticles impose a panmetabolic toxic effect along with strong necrosis, inducing activation of the envelope stress response in Salmonella enterica serovar Enteritidis.Antimicrobial agents and chemotherapy · 2015Article
- Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.Molecular microbiology · 2014Article
- Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.MicrobiologyOpen · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The natively disordered N-terminal 83-aa translocation (T) domain of E group nuclease colicins recruits OmpF to a colicin-receptor complex in the outer membrane (OM) as well as TolB in the periplasm of Escherichia coli, the latter triggering translocation of the toxin across the OM. We have identified the 16-residue TolB binding epitope in the natively disordered T-domain of the nuclease colicin E9 (ColE9) and solved the crystal structure of the complex. ColE9 folds into a distorted hairpin within a canyon of the six-bladed beta-propeller of TolB, using two tryptophans to bolt the toxin to the canyon floor and numerous intramolecular hydrogen bonds to stabilize the bound conformation. This mode of binding enables colicin side chains to hydrogen-bond TolB residues in and around the channel that runs through the beta-propeller and that constitutes the binding site of peptidoglycan-associated lipoprotein (Pal). Pal is a globular binding partner of TolB, and their association is known to be important for OM integrity. The structure is therefore consistent with translocation models wherein the colicin disrupts the TolB-Pal complex causing local instability of the OM as a prelude to toxin import. Intriguingly, Ca(2+) ions, which bind within the beta-propeller channel and switch the surface electrostatics from negative to positive, are needed for the negatively charged T-domain to bind TolB with an affinity equivalent to that of Pal and competitively displace it. Our study demonstrates that natively disordered proteins can compete with globular proteins for binding to folded scaffolds but that this can require cofactors such as metal ions to offset unfavorable interactions.
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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.