ArticleProceedings of the National Academy of Sciences of the United States of America2012
Apo-intermediate in the transport cycle of lactose permease (LacY).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Substrate-binding guides individual melibiose permeases MelB to structurally soften and to destabilize cytoplasmic middle-loop C3.Structure (London, England : 1993) · 2023Article
- Structural Insights into the Atomistic Mechanisms of Uric Acid Recognition and Translocation of Human Urate Anion Transporter 1.ACS omega · 2020Article
- Engineered occluded apo-intermediate of LacY.Proceedings of the National Academy of Sciences of the United States of America · 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
- Article
- Transient conformers of LacY are trapped by nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Observing a lipid-dependent alteration in single lactose permeases.Structure (London, England : 1993) · 2015Article
- Gating topology of the proton-coupled oligopeptide symporters.Structure (London, England : 1993) · 2015Article
- A chemiosmotic mechanism of symport.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Outward-facing conformers of LacY stabilized by nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Real-time conformational changes in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Substrate-induced changes in the structural properties of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Flexible gates generate occluded intermediates in the transport cycle of LacY.Journal of molecular biology · 2014Article
- Protonation drives the conformational switch in the multidrug transporter LmrP.Nature chemical biology · 2014Article
- Understanding transporter specificity and the discrete appearance of channel-like gating domains in transporters.Frontiers in pharmacology · 2014Review
- Structure-based mechanism for Na(+)/melibiose symport by MelB.Nature communications · 2014Article
- Evolutionary mix-and-match with MFS transporters II.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural insights into substrate recognition in proton-dependent oligopeptide transporters.EMBO reports · 2013Article
- Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The lactose permease (LacY) catalyzes coupled stoichiometric symport of a galactoside and an H(+). Crystal structures reveal 12, mostly irregular, transmembrane α-helices surrounding a cavity with sugar- and H(+)- binding sites at the apex, which is accessible from the cytoplasm and sealed on the periplasmic side (an inward-facing conformer). An outward-facing model has also been proposed based on biochemical and spectroscopic measurements, as well as the X-ray structure of a related symporter. Converging lines of evidence demonstrate that LacY functions by an alternating access mechanism. Here, we generate a model for an apo-intermediate of LacY based on crystallographic coordinates of LacY and the oligopeptide/H(+) symporter. The model exhibits a conformation with an occluded cavity inaccessible from either side of the membrane. Furthermore, kinetic considerations and double electron-electron resonance measurements suggest that another occluded conformer with bound sugar exists during turnover. An energy profile for symport is also presented.
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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.