Kanamycin-Mediated Conformational Dynamics of Escherichia coli Outer Membrane Protein TolC.

ABSTRACT: TolC is a member of the outer membrane efflux proteins (OEPs) family and acts as an exit duct to export proteins, antibiotics, and substrate molecules across the Escherichia coli cell membrane. Export of these molecules is evidenced to be brought about through the reversible interactions and binding of substrate-specific drug molecules or antibiotics with TolC and by being open for transport, which afterward leads to cross-resistance. Hence, the binding of kanamycin with TolC was monitored through molecular docking (MD), the structural fluctuations and conformational changes to the atomic level. The results were further supported from the steady-state fluorescence binding and isothermal titration calorimetry (ITC) studies. Binding of kanamycin with TolC resulted in a concentration d

SUBMITTER: Pattanayak BS 

PROVIDER: S-EPMC8083960 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature