Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768338 | Biochemical and Biophysical Research Communications | 2005 | 7 Pages |
Abstract
Suppressor of a groEL mutation protein E (SugE) is a small multidrug resistance (SMR) homologue. In comparison with other SMR proteins, SugE promotes bacterial resistance to a narrow range of quaternary ammonium compounds (QACs). Isothermal titration calorimetry was used to study the binding of QACs to Escherichia coli SugE in different membrane mimetic environments. In this study, the binding stoichiometry of SugE to drug was found to be 1:1, and the binding of SugE to drug was observed with the dissociation constant (KD) in the micromolar range for each of the drugs in the membrane mimetic environments explored. This interaction appears to be enthalpy-driven with enthalpies of 8-12Â kcal/mol for each of the drugs. These results are similar to those found with drug binding to the SMR protein EmrE in an earlier study.
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Authors
Curtis W. Sikora, Raymond J. Turner,