ArticleThe Journal of biological chemistry2015
Identification of a second substrate-binding site in solute-sodium symporters.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Functional characterization of SGLT1 using SSM-based electrophysiology: Kinetics of sugar binding and translocation.Frontiers in physiology · 2023Article
- A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport.The Journal of biological chemistry · 2021Article
- Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family.International journal of molecular sciences · 2021Review
- Allosteric regulation of mammalian NaNature structural & molecular biology · 2020Article
- The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
- Exploring Substrate Binding in the Extracellular Vestibule of MhsT by Atomistic Simulations and Markov Models.Journal of chemical information and modeling · 2018Article
- Article
- Core Transmembrane Domain 6 Plays a Pivotal Role in the Transport Cycle of the Sodium/Proline Symporter PutP.The Journal of biological chemistry · 2016Article
- Asymmetry in inward- and outward-affinity constant of transport explain unidirectional lysine flux in Saccharomyces cerevisiae.Scientific reports · 2016Article
- Stochastic steps in secondary active sugar transport.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Glu-311 in External Loop 4 of the Sodium/Proline Transporter PutP Is Crucial for External Gate Closure.The Journal of biological chemistry · 2016Article
- Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.Biochimica et biophysica acta · 2015Review
- Interaction of α-Lipoic Acid with the Human Na+/Multivitamin Transporter (hSMVT).The Journal of biological chemistry · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
The structure of the sodium/galactose transporter (vSGLT), a solute-sodium symporter (SSS) from Vibrio parahaemolyticus, shares a common structural fold with LeuT of the neurotransmitter-sodium symporter family. Structural alignments between LeuT and vSGLT reveal that the crystallographically identified galactose-binding site in vSGLT is located in a more extracellular location relative to the central substrate-binding site (S1) in LeuT. Our computational analyses suggest the existence of an additional galactose-binding site in vSGLT that aligns to the S1 site of LeuT. Radiolabeled galactose saturation binding experiments indicate that, like LeuT, vSGLT can simultaneously bind two substrate molecules under equilibrium conditions. Mutating key residues in the individual substrate-binding sites reduced the molar substrate-to-protein binding stoichiometry to ~1. In addition, the related and more experimentally tractable SSS member PutP (the Na(+)/proline transporter) also exhibits a binding stoichiometry of 2. Targeting residues in the proposed sites with mutations results in the reduction of the binding stoichiometry and is accompanied by severely impaired translocation of proline. Our data suggest that substrate transport by SSS members requires both substrate-binding sites, thereby implying that SSSs and neurotransmitter-sodium symporters share common mechanistic elements in substrate transport.
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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.