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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. doi:10.1016/j.bbamem.2011.07.017.

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 Creators:
Ganea, Constanta1, 2, Author           
Meyer-Lipp, Kerstin1, Author           
Lemonnier, R.3, Author
Krah, Alexander4, Author           
Leblanc, G.3, Author
Fendler, Klaus1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Department of Biophysics, Carol Davila Medical University, 050474 Bucharest, Romania, ou_persistent22              
3Institut de Biologie et de Technologies - Saclay, Service de Bioenergétique, Biologie Structurale et Méchanismes, Commissariat à l'Energie Atomique - Saclay, F-91191 Gif sur Yvette, France, ou_persistent22              
4Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              

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Free keywords: Solid supported membrane; Electrophysiology; Fluorescence spectroscopy; Kinetic model; Transport mechanism; Sugar transport
 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.

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Language(s): eng - English
 Dates: 2011-06-172011-03-022011-07-232011-07-232011-10-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbamem.2011.07.017
PMID: 21801712
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1808 (10) Sequence Number: - Start / End Page: 2508 - 2516 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702