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

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.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D5D6-6 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D5D7-4
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 Urheber:
Ganea, Constanta1, Autor           
Meyer-Lipp, Kerstin1, Autor           
Lemonnier, R., Autor
Krah, Alexander2, Autor           
Leblanc, G., Autor
Fendler, Klaus1, Autor           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              

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Schlagwörter: Solid supported membrane; Electrophysiology; Fluorescence spectroscopy; Kinetic model; Transport mechanism; Sugar transport
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2011-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 580295
 Art des Abschluß: -

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Titel: Biochimica et Biophysica Acta - Biomembranes
  Alternativer Titel : Biochim. Biophys. Acta (BBA) - Biomembranes
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 1808 (10) Artikelnummer: - Start- / Endseite: 2508 - 2516 Identifikator: -