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Article

Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies.

Biochemistry - 11 Oct 1994

Wu J, Kaback H R

Abstract excerpt

By using site-directed fluorescence spectroscopy, we have carried out structure/function studies on lactose permease purified from Escherichia coli in dodecyl beta, D-maltoside. Initially, permease containing a single native Cys at position 148 (helix V) was studied, since this residue is protected against alkylation by substrates of the permease. In the absence of ligand, Cys 148 permease reacts rapidly with...

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Identifiers

PMID: 7918438
DOI: 10.1021/bi00206a020

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies.PMID 7918438Read ↗

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Helices VII and X in the lactose permease of Escherichia coli: proximity and ligand-induced distance changes.Semantic proximity Read ↗

Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein.Semantic proximity Read ↗

Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport.Semantic proximity Read ↗

Ligand-induced movement of helix X in the lactose permease from Escherichia coli: a fluorescence quenching study.Semantic proximity Read ↗

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The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease.Semantic proximity Read ↗

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