Open AccessStructures suggest a mechanism for energy coupling by a family of organic anion transporters
Author(s) -
Jonathan B. Leano,
Samir Batarni,
Jacob Eriksen,
Narinobu Juge,
John E. Pak,
Tomomi KimuraSomeya,
Yaneth Robles-Colmenares,
Yoshinori Moriyama,
Robert M. Stroud,
Robert H. Edwards
Publication year - 2019
Publication title -
plos biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.127
H-Index - 271
eISSN - 1545-7885
pISSN - 1544-9173
DOI - 10.1371/journal.pbio.3000260
Subject(s) - symporter , cotransporter , biology , periplasmic space , permease , biochemistry , efflux , transporter , biophysics , antiporter , synaptic vesicle , neurotransmitter transporter , membrane transport protein , microbiology and biotechnology , vesicle , membrane , escherichia coli , chemistry , gene , organic chemistry , sodium
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.