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G117C MelB, a mutant melibiose permease with a changed conformational equilibrium

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Ganea,  Constanta
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Meyer-Lipp,  Kerstin
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Krah,  Alexander
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Ganea, C., Meyer-Lipp, K., Lemonnier, R., Krah, A., Leblanc, G., & Fendler, K. (2011). G117C MelB, a mutant melibiose permease with a changed conformational equilibrium. Biochimica et Biophysica Acta - Biomembranes, 1808(10), 2508-2516.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D5D6-6
Abstract
Replacement of the glycine at position 117 by a cysteine in the melibiose permease creates an interesting phenotype: while the mutant transporter shows still transport activity comparable to the wild type its pre steady-state kinetic properties are drastically altered. The transient charge displacements after substrate concentration jumps are strongly reduced and the fluorescence changes disappear. Together with its maintained transport activity this indicates that substrate translocation in G117C melibiose permease is not impaired but that the initial conformation of the mutant transporter differs from that of the wild type permease. A kinetic model for the G117C melibiose permease based on a rapid dynamic equilibrium of the substrate free transporter is proposed. Implications of the kinetic model for the transport mechanism of the wild type permease are discussed.