Structures suggest a mechanism for energy coupling by a family of organic anion transporters

Jonathan B. Leano, Samir Batarni, Jacob Eriksen, Narinobu Juge, John E. Pak, Tomomi Kimura-Someya, Yaneth Robles-Colmenares, Yoshinori Moriyama, Robert M. Stroud, Robert H. Edwards

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article numbere3000260
JournalPLoS biology
Volume17
Issue number5
DOIs
Publication statusPublished - May 2019
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Agricultural and Biological Sciences(all)

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