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Article

Real-time conformational changes in LacY.

Proceedings of the National Academy of Sciences of the United States of America - 10 Jun 2014

Smirnova Irina, Kasho Vladimir, Kaback H Ronald

Abstract excerpt

Galactoside/H(+) symport across the cytoplasmic membrane of Escherichia coli is catalyzed by lactose permease (LacY), which uses an alternating access mechanism with opening and closing of deep cavities on the periplasmic and cytoplasmic sides. In this study, conformational changes in LacY initiated by galactoside binding were monitored in real time by Trp quenching/unquenching of bimane, a small fluorophore...

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Identifiers

PMID: 24872451
DOI: 10.1073/pnas.1408374111
PMCID: PMC4060661

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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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Real-time conformational changes in LacY.PMID 24872451Read ↗

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Residues gating the periplasmic pathway of LacY.Semantic proximity Read ↗

Outward-facing conformers of LacY stabilized by nanobodies.Semantic proximity Read ↗

Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation.Semantic proximity Read ↗

Crystal Structure of a ligand-bound LacY-Nanobody Complex.Semantic proximity Read ↗

Sugar binding induces an outward facing conformation of LacY.Semantic proximity Read ↗

Delineating electrogenic reactions during lactose/H+ symport.Semantic proximity Read ↗

Role of protons in sugar binding to LacY.Semantic proximity Read ↗

Evidence for an intermediate conformational state of LacY.Semantic proximity Read ↗

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