Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin.

ABSTRACT: VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS_AR_A two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS_A sensory component has not hitherto been identified. Here we employ purified, intact and active VanS_A membrane protein (henceforth referred to as VanS) in analytical ultracentrifugation experiments to study VanS oligomeric state and conformation in the absence and presence of vancomycin. A combination of sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge (SEDFIT, SEDFIT-MSTAR and MULTISIG analysis) showed that VanS in the absence of the ligand is almost entirely monomeric (molar mass M = 45.7 kDa) in dilut

SUBMITTER: Phillips-Jones MK 

PROVIDER: S-EPMC5387412 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature