ArticleMolecular bioSystems2010
The sodium/galactose symporter crystal structure is a dynamic, not so occluded state.
Article in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Mapping of Ion and Substrate Binding Sites in Human Sodium Iodide Symporter (hNIS).Journal of chemical information and modeling · 2020Article
- Na+ coordination at the Na2 site of the Na+/I- symporter.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Stochastic steps in secondary active sugar transport.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Microscopic Characterization of Membrane Transporter Function by In Silico Modeling and Simulation.Methods in enzymology · 2016Review
- Identification of a second substrate-binding site in solute-sodium symporters.The Journal of biological chemistry · 2015Article
- Metadynamics simulations reveal a Na+ independent exiting path of galactose for the inward-facing conformation of vSGLT.PLoS computational biology · 2014Article
- Complete mapping of substrate translocation highlights the role of LeuT N-terminal segment in regulating transport cycle.PLoS computational biology · 2014Article
- Functional identification and characterization of sodium binding sites in Na symporters.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.Biophysical journal · 2013Article
- Visualizing functional motions of membrane transporters with molecular dynamics simulations.Biochemistry · 2013Review
- Investigation of the sodium-binding sites in the sodium-coupled betaine transporter BetP.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/γ-butyrobetaine antiporter CaiT.The Journal of biological chemistry · 2012Article
- A gate-free pathway for substrate release from the inward-facing state of the Na⁺-galactose transporter.Biochimica et biophysica acta · 2012Article
- The structural pathway for water permeation through sodium-glucose cotransporters.Biophysical journal · 2011Article
- Conserved tyrosine in the first transmembrane segment of solute:sodium symporters is involved in Na+-coupled substrate co-transport.The Journal of biological chemistry · 2011Article
- The mechanism of substrate release by the aspartate transporter GltPh: insights from simulations.Molecular bioSystems · 2011Article
- Water permeation through the sodium-dependent galactose cotransporter vSGLT.Biophysical journal · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The recent elucidation of the sodium/galactose symporter structure from the Vibrio parahaemolyticus bacterium, vSGLT, has revealed a similarity in the core architecture with transporters from different gene families, including the leucine transporter (LeuT). Even though several transporters sharing this core have been structurally determined over the past few years, vSGLT is the only one crystallized in the substrate-bound inward-facing conformation so far. In this study, we report the first insight into the dynamics and coordination of the galactose (Gal) and proposed Na+ ion in vSGLT using a series of molecular dynamics simulations with a total time of about 0.1 micros. Our study reveals new residues, not observed in the crystal structure, which closely interact with the Na(+) ion or the substrate for extended times, and shows that in the crystallized conformation, a Na+ ion placed at the site equivalent to Na2 in LeuT can escape into the intracellular (IC) space in the absence of external forces. We have identified the highly conserved Asp189 as a likely binding residue on the pathway of Na(+) into the IC cavity. The release of Gal, on the other hand, requires the rotation of the side chain of the inner hydrophobic gate, Tyr263, without a significant change in vSGLT backbone conformation. Our simulations further show that the crystal structure represents but one accessible binding pose of Gal and Na+ among an ensemble of microstates, and that the Gal undergoes versatile alternate interactions at the binding pocket.
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