Evidence for the Supramolecular Organization of a Bacterial Outer-Membrane Protein from In Vivo Pulse Electron Paramagnetic Resonance Spectroscopy
| Autor: | David S. Cafiso, Kateri H. DuBay, Thushani D. Nilaweera, David A. Nyenhuis, Jessica K Niblo, Nhu Q Nguyen |
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| Rok vydání: | 2020 |
| Předmět: |
Macromolecular Substances
Supramolecular chemistry Molecular Dynamics Simulation 010402 general chemistry medicine.disease_cause 01 natural sciences Biochemistry Catalysis Article law.invention chemistry.chemical_compound Colloid and Surface Chemistry law Gram-Negative Bacteria medicine Electron paramagnetic resonance Escherichia coli Molecular Structure Intermolecular force Electron Spin Resonance Spectroscopy General Chemistry 0104 chemical sciences Monomer Membrane chemistry Membrane protein Biophysics Bacterial outer membrane Monte Carlo Method Bacterial Outer Membrane Proteins |
| Zdroj: | J Am Chem Soc |
| ISSN: | 1520-5126 |
| Popis: | In the outer membrane of Gram-negative bacteria, membrane proteins are thought to be organized into domains or islands that play a role in the segregation, movement, and turnover of membrane components. However, there is presently limited information on the structure of these domains or the molecular interactions that mediate domain formation. In the present work, the Escherichia coli outer membrane vitamin B12 transporter, BtuB, was spin-labeled, and double electron-electron resonance was used to measure the distances between proteins in intact cells. These data together with Monte Carlo simulations provide evidence for the presence of specific intermolecular contacts between BtuB monomers that could drive the formation of string-like oligomers. Moreover, the EPR data provide evidence for the location of the interacting interfaces and indicate that lipopolysaccharide mediates the contacts between BtuB monomers. |
| Databáze: | OpenAIRE |
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