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Article

Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane.

Proceedings of the National Academy of Sciences of the United States of America - 25 May 2010

Nie Yiling, Kaback H Ronald

Abstract excerpt

Many independent lines of evidence indicate that the lactose permease of Escherichia coli (LacY) is highly dynamic and that sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport catalyzed by LacY very...

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Identifiers

PMID: 20457922
DOI: 10.1073/pnas.1004515107
PMCID: PMC2906848

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20457922-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane.PMID 20457922Read ↗

Single-molecule FRET reveals sugar-induced conformational dynamics in LacY.Semantic proximity Read ↗

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

Real-time conformational changes in LacY.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 ↗

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

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

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

Structure and mechanism of the lactose permease of Escherichia coli.Semantic proximity Read ↗

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

Site-directed alkylation of cysteine to test solvent accessibility of membrane proteins.Semantic proximity Read ↗

YidC protein, a molecular chaperone for LacY protein folding via the SecYEG protein machinery.Semantic proximity Read ↗

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