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| Home > Publications database > Transport mechanism of DgoT, a bacterial homolog of SLC17 organic anion transporters |
| Typ | Amount | VAT | Currency | Share | Status | Cost centre |
| APC | 3000.00 | 0.00 | EUR | 46.22 % | (Zahlung erfolgt) | ZB |
| APC | 3490.00 | 0.00 | EUR | 53.78 % | (Zahlung angewiesen) | 44500 |
| Sum | 6490.00 | 0.00 | EUR | |||
| Total | 6490.00 |
| Journal Article | FZJ-2025-01830 |
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2024
Nature Publishing Group UK
[London]
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Please use a persistent id in citations: doi:10.1038/s44318-024-00279-y doi:10.34734/FZJ-2025-01830
Abstract: The solute carrier 17 (SLC17) family contains anion transportersthat accumulate neurotransmitters in secretory vesicles, removecarboxylated monosaccharides from lysosomes, or extrude organicanions from the kidneys and liver.We combined classical moleculardynamics simulations, Markov state modeling and hybrid firstprinciples quantum mechanical/classical mechanical (QM/MM)simulations with experimental approaches to describe the transportmechanisms of a model bacterial protein, the D-galactonatetransporter DgoT, at atomic resolution. We found that protonationof D46 and E133 precedes galactonate binding and that substratebinding induces closure of the extracellular gate, with the conservedR47 coupling substrate binding to transmembrane helixmovement. After isomerization to an inward-facing conformation,deprotonation of E133 and subsequent proton transfer from D46 toE133 opens the intracellular gate and permits galactonate dissociationeither in its unprotonated form or after proton transferfrom E133. After release of the second proton, apo DgoT returns tothe outward-facing conformation. Our results provide a frameworkto understand how various SLC17 transport functions with distincttransport stoichiometries can be attained through subtle variationsin proton and substrate binding/unbinding.
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