ArticleThe Journal of biological chemistry2011
Redesign of a plugged beta-barrel membrane protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 68 citations in OpenAlex.
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- Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules.Microbial biotechnology · 2025Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- Real-Time Measurement of a Weak Interaction of a Transcription Factor Motif with a Protein Hub at Single-Molecule Precision.ACS nano · 2024Article
- Review
- Inhibitor of Chromosome Segregation inACS chemical biology · 2024Article
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Dissecting the Permeability of theACS omega · 2023Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Article
- A generalizable nanopore sensor for highly specific protein detection at single-molecule precision.Nature communications · 2023Article
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- Disentangling the recognition complexity of a protein hub using a nanopore.Nature communications · 2022Article
- Supramolecular assembly of protein building blocks: from folding to function.Nano convergence · 2022Review
- Recent advances in integrated solid-state nanopore sensors.Lab on a chip · 2021Review
- Outer membrane protein evolution.Current opinion in structural biology · 2021Review
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021Article
- Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The redesign of biological nanopores is focused on bacterial outer membrane proteins and pore-forming toxins, because their robust β-barrel structure makes them the best choice for developing stochastic biosensing elements. Using membrane protein engineering and single-channel electrical recordings, we explored the ferric hydroxamate uptake component A (FhuA), a monomeric 22-stranded β-barrel protein from the outer membrane of Escherichia coli. FhuA has a luminal cross-section of 3.1 × 4.4 nm and is filled by a globular N-terminal cork domain. Various redesigned FhuA proteins were investigated, including single, double, and multiple deletions of the large extracellular loops and the cork domain. We identified four large extracellular loops that partially occlude the lumen when the cork domain is removed. The newly engineered protein, FhuAΔC/Δ4L, was the result of a removal of almost one-third of the total number of amino acids of the wild-type FhuA (WT-FhuA) protein. This extensive protein engineering encompassed the entire cork domain and four extracellular loops. Remarkably, FhuAΔC/Δ4L forms a functional open pore in planar lipid bilayers, with a measured unitary conductance of ∼4.8 nanosiemens, which is much greater than the values recorded previously with other engineered FhuA protein channels. There are numerous advantages and prospects of using such an engineered outer membrane protein not only in fundamental studies of membrane protein folding and design, and the mechanisms of ion conductance and gating, but also in more applicative areas of stochastic single-molecule sensing of proteins and nucleic acids.
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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.