ArticleStructure (London, England : 1993)2012
Proton-coupled dynamics in lactose permease.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 59 citations in OpenAlex.
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- Proton-Binding Motifs of Membrane-Bound Proteins: From Bacteriorhodopsin to Spike Protein S.Frontiers in chemistry · 2021Article
- Structural and Functional Adaptability of Sucrose and Lactose Permeases fromBiochemistry · 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
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Phylogenetic and conservation analyses of MFS transporters.3 Biotech · 2018Article
- Direct protein-lipid interactions shape the conformational landscape of secondary transporters.Nature communications · 2018Article
- Uptake dynamics in the Lactose permease (LacY) membrane protein transporter.Scientific reports · 2018Article
- Proton movement and coupling in the POT family of peptide transporters.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae.Scientific reports · 2017Article
- pKProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Key Residues and Phosphate Release Routes in the Saccharomyces cerevisiae Pho84 Transceptor: THE ROLE OF TYR179 IN FUNCTIONAL REGULATION.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Lactose permease of Escherichia coli (LacY) catalyzes symport of a galactopyranoside and an H⁺ via an alternating access mechanism. The transition from an inward- to an outward-facing conformation of LacY involves sugar-release followed by deprotonation. Because the transition depends intimately upon the dynamics of LacY in a bilayer environment, molecular dynamics (MD) simulations may be the only means of following the accompanying structural changes in atomic detail. Here, we describe MD simulations of wild-type apo LacY in phosphatidylethanolamine (POPE) lipids that features two protonation states of the critical Glu325. While the protonated system displays configurational stability, deprotonation of Glu325 causes significant structural rearrangements that bring into proximity side chains important for H⁺ translocation and sugar binding and closes the internal cavity. Moreover, protonated LacY in phosphatidylcholine (DMPC) lipids shows that the observed dynamics are lipid-dependent. Together, the simulations describe early dynamics of the inward-to-outward transition of LacY that agree well with experimental data.
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