ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of sugar-bound LacY.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
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- Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mobile barrier mechanisms for NaeLife · 2024Article
- Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023Article
- Lactose Permease Scrambles Phospholipids.Biology · 2023Article
- Cooperative binding ensures the obligatory melibiose/Na+ cotransport in MelB.The Journal of general physiology · 2021Article
- X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB.Communications biology · 2021Article
- Function Trumps Form in Two Sugar Symporters,International journal of molecular sciences · 2021Review
- Structural Insights into the Atomistic Mechanisms of Uric Acid Recognition and Translocation of Human Urate Anion Transporter 1.ACS omega · 2020Article
- Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.Scientific reports · 2020Article
- The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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- Hydrogen-Deuterium Exchange Mass-Spectrometry of Secondary Active Transporters: From Structural Dynamics to Molecular Mechanisms.Frontiers in pharmacology · 2020Review
- The lipid-dependent structure and function of LacY can be recapitulated and analyzed in phospholipid-containing detergent micelles.Scientific reports · 2019Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Variation of a major facilitator superfamily gene contributes to differential cadmium accumulation between rice subspecies.Nature communications · 2019Article
- Conformational Studies of Glucose Transporter 1 (GLUT1) as an Anticancer Drug Target.Molecules (Basel, Switzerland) · 2019Article
11 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
Here we describe the X-ray crystal structure of a double-Trp mutant (Gly46→Trp/Gly262→Trp) of the lactose permease of Escherichia coli (LacY) with a bound, high-affinity lactose analog. Although thought to be arrested in an open-outward conformation, the structure is almost occluded and is partially open to the periplasmic side; the cytoplasmic side is tightly sealed. Surprisingly, the opening on the periplasmic side is sufficiently narrow that sugar cannot get in or out of the binding site. Clearly defined density for a bound sugar is observed at the apex of the almost occluded cavity in the middle of the protein, and the side chains shown to ligate the galactopyranoside strongly confirm more than two decades of biochemical and spectroscopic findings. Comparison of the current structure with a previous structure of LacY with a covalently bound inactivator suggests that the galactopyranoside must be fully ligated to induce an occluded conformation. We conclude that protonated LacY binds D-galactopyranosides specifically, inducing an occluded state that can open to either side of the membrane.
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