ArticleThe Journal of biological chemistry2012
Low resolution structure and dynamics of a colicin-receptor complex determined by neutron scattering.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Complex Structural Examination of Protein-Lipid Interactions with Neutron Scattering Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Small-angle x-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model.Biophysical journal · 2023Article
- Exploiting neutron scattering contrast variation in biological membrane studies.Biophysics reviews · 2022Review
- Pore Forming Protein Induced Biomembrane Reorganization and Dynamics: A Focused Review.Frontiers in molecular biosciences · 2021Review
- Studying the surfaces of bacteria using neutron scattering: finding new openings for antibiotics.Biochemical Society transactions · 2020Review
- Study of the Mechanism of the Antimicrobial Activity of Novel Water Soluble Ammonium Quaternary Benzanthrone on Model Membranes.The Journal of membrane biology · 2020Article
- Determining the amphipol distribution within membrane-protein fibre samples using small-angle neutron scattering.Acta crystallographica. Section D, Structural biology · 2018Article
- Solution Structure of an Intramembrane Aspartyl Protease via Small Angle Neutron Scattering.Biophysical journal · 2018Article
- Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data.Biophysical journal · 2017Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- Coupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1.Biophysical journal · 2017Article
- Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.The journal of physical chemistry letters · 2017Article
- Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Effect of Lipopolysaccharide Core Oligosaccharide Size on the Electrostatic Binding of Antimicrobial Proteins to Models of the Gram Negative Bacterial Outer Membrane.Langmuir : the ACS journal of surfaces and colloids · 2016Article
- An Accurate In Vitro Model of theAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2015Article
- An accurate in vitro model of the E. coli envelope.Angewandte Chemie (International ed. in English) · 2015Article
- Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDI.Applied and environmental microbiology · 2015Article
- Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.Microbiology (Reading, England) · 2015Article
- Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.The Journal of biological chemistry · 2015Article
- Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals.The Journal of membrane biology · 2014Article
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Authors and funding
11 authors.
Funding
Abstract
Proteins that translocate across cell membranes need to overcome a significant hydrophobic barrier. This is usually accomplished via specialized protein complexes, which provide a polar transmembrane pore. Exceptions to this include bacterial toxins, which insert into and cross the lipid bilayer itself. We are studying the mechanism by which large antibacterial proteins enter Escherichia coli via specific outer membrane proteins. Here we describe the use of neutron scattering to investigate the interaction of colicin N with its outer membrane receptor protein OmpF. The positions of lipids, colicin N, and OmpF were separately resolved within complex structures by the use of selective deuteration. Neutron reflectivity showed, in real time, that OmpF mediates the insertion of colicin N into lipid monolayers. This data were complemented by Brewster Angle Microscopy images, which showed a lateral association of OmpF in the presence of colicin N. Small angle neutron scattering experiments then defined the three-dimensional structure of the colicin N-OmpF complex. This revealed that colicin N unfolds and binds to the OmpF-lipid interface. The implications of this unfolding step for colicin translocation across membranes are discussed.
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