Article
Dihydrostreptomycin Directly Binds to, Modulates, and Passes through the MscL Channel Pore.
PLoS biology - 1 Jun 2016
Wray Robin, Iscla Irene, Gao Ya, Li Hua, Wang Junmei, Blount Paul
Abstract excerpt
The primary mechanism of action of the antibiotic dihydrostreptomycin is binding to and modifying the function of the bacterial ribosome, thus leading to decreased and aberrant translation of proteins; however, the routes by which it enters the bacterial cell are largely unknown. The mechanosensitive channel of large conductance, MscL, is found in the vast majority of bacterial species, where it serves as an...
Topics
- Anti-Bacterial Agents
- Binding Sites
- Cell Membrane
- Cysteine
- Dihydrostreptomycin Sulfate
- Escherichia coli
- Escherichia coli Proteins
- Glutamic Acid
- Ion Channel Gating
- Ion Channels
- Mechanoreceptors
- Molecular Docking Simulation
- Molecular Dynamics Simulation
- Mutation
- Potassium
- Protein Binding
- Protein Conformation