Ligand‐Induced conformational changes in the lactose permease of escherichia coli: Evidence for two binding sites

By using a lactose permease mutant containing a single Cys residue in place of Val 331 (helix X), conformational changes induced by ligand binding were studied. With right‐side‐out membrane vesicles containing Val 331 → Cys permease, lactose transport is inactivated by either N‐ethylmaleimide (NEM)...

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Veröffentlicht in:	Protein science 1994-12, Vol.3 (12), p.2294-2301
Hauptverfasser:	Wu, Jianhua, Frillingos, Stathis, Voss, John, Ronald Kaback, H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anilino Naphthalenesulfonates - pharmacology Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Coumarins - pharmacology Cysteine - chemistry C‐less permease Electron Spin Resonance Spectroscopy Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins Ethylmaleimide - pharmacology Isopropyl Thiogalactoside - pharmacology Lactose - metabolism Ligands ligand‐protein interaction Membrane Transport Modulators Membrane Transport Proteins - antagonists & inhibitors Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism MIANS Molecular Sequence Data Monosaccharide Transport Proteins Mutagenesis, Site-Directed Protein Conformation - drug effects Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism site‐directed fluorescence site‐directed spin labeling Spectrometry, Fluorescence Spin Labels Symporters Thiogalactosides - pharmacology Valine - chemistry
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