ArticleBiophysical journal2007
Sugar transport across lactose permease probed by steered molecular dynamics.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 67 citations in OpenAlex.
- Structural insights into a conserved mechanism of choline translocation through CHT.Science advances · 2026Article
- Uptake dynamics in the Lactose permease (LacY) membrane protein transporter.Scientific reports · 2018Article
- Computational Studies of Molecular Permeation through Connexin26 Channels.Biophysical journal · 2016Article
- Computing Protein-Protein Association Affinity with Hybrid Steered Molecular Dynamics.Journal of chemical theory and computation · 2015Article
- Hybrid Steered Molecular Dynamics Approach to Computing Absolute Binding Free Energy of Ligand-Protein Complexes: A Brute Force Approach That Is Fast and Accurate.Journal of chemical theory and computation · 2015Article
- Computing membrane-AQP5-phosphatidylserine binding affinities with hybrid steered molecular dynamics approach.Molecular membrane biology · 2015Article
- Unveiling the gating mechanism of ECF transporter RibU.Scientific reports · 2013Article
- Visualizing functional motions of membrane transporters with molecular dynamics simulations.Biochemistry · 2013Review
- Article
- A steered molecular dynamics study of binding and translocation processes in the GABA transporter.PloS one · 2012Article
- Lactose permease and the alternating access mechanism.Biochemistry · 2011Article
- The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter.PloS one · 2011Article
- Elucidation of the glucose transport pathway in glucose transporter 4 via steered molecular dynamics simulations.PloS one · 2011Article
- Probing the periplasmic-open state of lactose permease in response to sugar binding and proton translocation.Journal of molecular biology · 2010Article
- Residues gating the periplasmic pathway of LacY.Journal of molecular biology · 2009Article
- Article
- Molecular dynamics simulations of membrane channels and transporters.Current opinion in structural biology · 2009Review
- The mechanism of a neurotransmitter:sodium symporter--inward release of Na+ and substrate is triggered by substrate in a second binding site.Molecular cell · 2008Article
- Substrate binding and formation of an occluded state in the leucine transporter.Biophysical journal · 2008Article
- Amino acids that confer transport of raffinose and maltose sugars in the raffinose permease (RafB) of Escherichia coli as implicated by spontaneous mutations at Val-35, Ser-138, Ser-139, Gly-389 and Ile-391.The Journal of membrane biology · 2007Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Escherichia coli lactose permease (LacY) transports sugar across the inner membrane of the bacterium using the proton motive force to accumulate sugar in the cytosol. We have probed lactose conduction across LacY using steered molecular dynamics, permitting us to follow molecular and energetic details of lactose interaction with the lumen of LacY during its permeation. Lactose induces a widening of the narrowest parts of the channel during permeation, the widening being largest within the periplasmic half-channel. During permeation, the water-filled lumen of LacY only partially hydrates lactose, forcing it to interact with channel lining residues. Lactose forms a multitude of direct sugar-channel hydrogen bonds, predominantly with residues of the flexible N-domain, which is known to contribute a major part of LacY's affinity for lactose. In the periplasmic half-channel lactose predominantly interacts with hydrophobic channel lining residues, whereas in the cytoplasmic half-channel key protein-substrate interactions are mediated by ionic residues. A major energy barrier against transport is found within a tight segment of the periplasmic half-channel where sugar hydration is minimal and protein-sugar interaction maximal. Upon unbinding from the binding pocket, lactose undergoes a rotation to permeate either half-channel with its long axis aligned parallel to the channel axis. The results hint at the possibility of a transport mechanism, in which lactose permeates LacY through a narrow periplasmic half-channel and a wide cytoplasmic half-channel, the opening of which is controlled by changes in protonation states of key protein side groups.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.