Studies of the ATP-binding Cassette MalK of the Maltose ABC Transporter MalFGK2 and Its Inhibitor EIIA.

Studies of the ATP-binding Cassette MalK of the Maltose ABC Transporter MalFGK2 and Its Inhibitor EIIA.

139 pages· 2007· ISBN 9780549563006
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EIIAGlc is a key component of the glucose-specific phosphoenolpyruvate: carbohydrate phosphotransferase system (PTS). When glucose is present, EIIA Glc is unphosphorylated, and inhibits certain sugar transporters including MalFGK2 in a process called inducer exclusion. The interaction between EIIAGlc and MalFGK2 was studied using various biochemical and biophysical methods, including a binding assay with fluorescence anisotropy, an inhibition assay, and X-ray crystallography. Zn2+ was found to greatly increase the dissociation constant of MalFGK2 and EIIAGlc. In addition, EIIAGlc binds to MalFGK 2 in the ground state more favorably than in the transition state. This Zn2+-promoted interaction between EIIAGlc and MalFGK2 may be physiologically relevant.

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