PLoS biology, 2019-05, Vol.17 (5), p.e3000260-e3000260
2019
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- Autor(en) / Beteiligte
- Titel
- Structures suggest a mechanism for energy coupling by a family of organic anion transporters
- Ist Teil von
- PLoS biology, 2019-05, Vol.17 (5), p.e3000260-e3000260
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2019
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1545-7885, 1544-9173eISSN: 1545-7885DOI: 10.1371/journal.pbio.3000260Titel-ID: cdi_plos_journals_2249977557
- Format
- –
- Schlagworte
- Acids, Anions, Biochemistry, Biological Transport, Biology and Life Sciences, Biophysics, Coupling, Departments, E coli, Efflux, Energy coupling, Energy Metabolism, Escherichia coli - metabolism, Escherichia coli Proteins - chemistry, Escherichia coli Proteins - metabolism, Hydrogen, Medicine, Membrane potential, Models, Molecular, Neurology, Neurotransmitters, Organic Anion Transporters - chemistry, Organic Anion Transporters - metabolism, Physical Sciences, Physiology, Protein Conformation, Proteins, Protons, Substrates, Sugar Acids - metabolism, Synaptic vesicles