ArticleBiophysical journal2010
Conformational rearrangements to the intracellular open states of the LeuT and ApcT transporters are modulated by common mechanisms.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Exploring the Structural Dynamics of LeuT Using EPR Spectroscopy: A Focus on Transmembrane Helix 10.Journal of neurochemistry · 2025Article
- Sodium/Iodide Symporter Metastable Intermediates Provide Insights into Conformational Transition between Principal Thermodynamic States.The journal of physical chemistry. B · 2023Article
- Molecular Mechanism of Nramp-Family Transition Metal Transport.Journal of molecular biology · 2021Review
- The fine art of preparing membrane transport proteins for biomolecular simulations: Concepts and practical considerations.Methods (San Diego, Calif.) · 2021Review
- Computation-guided analysis of paroxetine binding to hSERT reveals functionally important structural elements and dynamics.Neuropharmacology · 2019Article
- Article
- The LeuT-fold neurotransmitter:sodium symporter MhsT has two substrate sites.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Insights into the Structure, Function, and Ligand Discovery of the Large Neutral Amino Acid Transporter 1, LAT1.International journal of molecular sciences · 2018Review
- The Isomeric Preference of an Atypical Dopamine Transporter Inhibitor Contributes to Its Selection of the Transporter Conformation.ACS chemical neuroscience · 2017Article
- A novel proton transfer mechanism in the SLC11 family of divalent metal ion transporters.Scientific reports · 2017Article
- The role of transmembrane segment 5 (TM5) in Na2 release and the conformational transition of neurotransmitter:sodium symporters toward the inward-open state.The Journal of biological chemistry · 2017Article
- The Environment Shapes the Inner Vestibule of LeuT.PLoS computational biology · 2016Article
- Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter:sodium symporter.The Journal of biological chemistry · 2015Article
- Conformational cycle and ion-coupling mechanism of the Na+/hydantoin transporter Mhp1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Not just an oil slick: how the energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins.Biophysical journal · 2014Review
- Physiological sodium concentrations enhance the iodide affinity of the Na+/I- symporter.Nature communications · 2014Article
- Conformational dynamics of ligand-dependent alternating access in LeuT.Nature structural & molecular biology · 2014Article
- The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transport.The Journal of biological chemistry · 2014Article
- The molecular mechanism of ion-dependent gating in secondary transporters.PLoS computational biology · 2013Article
- Chloride binding site of neurotransmitter sodium symporters.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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2 authors.
Funding
Abstract
Recent crystallographic studies revealed that five transporter families without much sequence similarities among them have similar structure folds to LeuT, a bacterial neurotransmitter:sodium symporter homolog. The LeuT fold is characterized by an internal twofold structural pseudosymmetry. The transport cycle of some members of each of these families is dependent on a sodium gradient across the membrane, whereas in some others the role of sodium is mimicked by proton. We report on the identification of common structure-dynamics elements of the transporters with LeuT fold, which are recognizable in the conformational transitions related to function. The findings from comparative computational modeling and simulation studies of LeuT, and ApcT from the amino acid-polyamine-organocation transporter family define the intramolecular mechanisms by which Na+ binding couples to the transport process, and single out the lead/active role of TM1a in the transition to inward-open conformation. These mechanistic insights are derived in the context of collaborative investigations of LeuT dynamics with both single-molecule fluorescence and simulations that have produced excellent agreement of the dynamic details, and are found to be generalizable across the transporter families and to transcend sequence and motif similarities.
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